Identification

Name
Pyridoxal Phosphate
Accession Number
DB00114  (NUTR00045)
Type
Small Molecule
Groups
Nutraceutical
Description

This is the active form of vitamin B6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (pyridoxamine). [PubChem]

Structure
Thumb
Synonyms
  • 3-hydroxy-2-methyl-5-((phosphonooxy)methyl)-4-pyridinecarboxaldehyde
  • 3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphate
  • Codecarboxylase
  • PLP
  • Pyridoxal 5-monophosphoric acid ester
  • Pyridoxal 5-phosphate
  • Pyridoxal 5'-phosphate
  • Pyridoxal P
  • Pyridoxal phosphate anhydrous
  • Pyridoxal-5P
  • Pyridoxal-P
Product Ingredients
IngredientUNIICASInChI Key
Pyridoxal phosphate hydrate5V5IOJ833841468-25-1CEEQUQSGVRRXQI-UHFFFAOYSA-N
International/Other Brands
Biosechs / Himitan / Vitazechs
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing End
EnBrace HRPyridoxal Phosphate (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (25 ug/1) + Folic Acid (1 mg/1) + Glycine betaine (500 ug/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (5.23 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Magnesium L-threonate (1 mg/1) + Magnesium ascorbate (24 mg/1) + Zinc ascorbate (1 mg/1)Capsule, delayed release pelletsOralJaymac Pharmaceuticals, Llc2015-04-08Not applicableUs
EnLytePyridoxal Phosphate (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Citric acid monohydrate (1.83 mg/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (25 ug/1) + Folic Acid (1 mg/1) + Glycine betaine (500 ug/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (7 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Sodium Citrate (3.67 mg/1) + Magnesium L-threonate (1 mg/1) + Magnesium ascorbate (24 mg/1) + Zinc ascorbate (1 mg/1)Capsule, delayed release pelletsOralJaymac Pharmaceuticals Llc2011-10-01Not applicableUs
Categories
UNII
F06SGE49M6
CAS number
54-47-7
Weight
Average: 247.1419
Monoisotopic: 247.024573569
Chemical Formula
C8H10NO6P
InChI Key
NGVDGCNFYWLIFO-UHFFFAOYSA-N
InChI
InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
IUPAC Name
[(4-formyl-5-hydroxy-6-methylpyridin-3-yl)methoxy]phosphonic acid
SMILES
CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O

Pharmacology

Indication

For nutritional supplementation and for treating dietary shortage or imbalance.

Structured Indications
Not Available
Pharmacodynamics

The two major forms of vitamin B6 are pyridoxine and pyridoxamine. In the liver they are converted to pyridoxal phosphate (PLP) which is a cofactor in many reactions of amino acid metabolism. PLP also is necessary for the enzymatic reaction governing the release of glucose from glycogen. Pyroluria is one potential cause of vitamin B6 deficiency.

Mechanism of action

Pyridoxal Phosphate is a coenzyme of many enzymatic reactions. It is the active form of vitamin B6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine. Pyridoxal phosphate acts as a coenzyme in all transamination reactions, and in some decarboxylation and deamination reactions of amino acids. The aldehyde group of pyridoxal phosphate forms a Schiff-base linkage with the epsilon-amino group of a specific lysine group of the aminotransferase enzyme. The alpha-amino group of the amino acid substrate displaces the epsilon-amino group of the active-site lysine residue. The resulting aldimine becomes deprotonated to become a quinoid intermediate, which in turn accepts a proton at a different position to become a ketimine. The resulting ketimine is hydrolysed so that the amino group remains on the protein complex.

TargetActionsOrganism
UAlanine--glyoxylate aminotransferase 2, mitochondrial
cofactor
Human
UGlutamate decarboxylase 1
cofactor
Human
UCystathionine beta-synthase
cofactor
Human
UKynureninase
cofactor
Human
USerine hydroxymethyltransferase, cytosolic
cofactor
Human
UCysteine desulfurase, mitochondrial
cofactor
Human
UAspartate aminotransferase, cytoplasmic
activator
Human
UOrnithine aminotransferase, mitochondrial
cofactor
Human
UOrnithine decarboxylase
cofactor
Human
UKynurenine/alpha-aminoadipate aminotransferase, mitochondrial
cofactor
Human
U4-aminobutyrate aminotransferase, mitochondrial
inhibitor
Human
UPyridoxine-5'-phosphate oxidase
cofactor
Human
USphingosine-1-phosphate lyase 1
cofactor
Human
UTyrosine aminotransferase
cofactor
Human
UKynurenine--oxoglutarate transaminase 1
cofactor
Human
UThreonine synthase-like 1
cofactor
Human
UGlycogen phosphorylase, liver form
cofactor
Human
USerine palmitoyltransferase 2
cofactor
Human
UCysteine sulfinic acid decarboxylase
cofactor
Human
UHistidine decarboxylase
cofactor
Human
UArginine decarboxylase
cofactor
Human
UL-serine dehydratase/L-threonine deaminase
cofactor
Human
U2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
cofactor
Human
UGlycine dehydrogenase [decarboxylating], mitochondrial
cofactor
Human
UAlanine aminotransferase 1
cofactor
Human
UPhosphoserine aminotransferase
cofactor
Human
U5-aminolevulinate synthase, nonspecific, mitochondrial
cofactor
Human
USerine--pyruvate aminotransferase
cofactor
Human
UPyridoxal phosphate phosphatase
cofactor
Human
USerine palmitoyltransferase 1
cofactor
Human
UCystathionine gamma-lyase
cofactor
Human
UBranched-chain-amino-acid aminotransferase, cytosolic
cofactor
Human
UBranched-chain-amino-acid aminotransferase, mitochondrial
cofactor
Human
UProline synthase co-transcribed bacterial homolog protein
cofactor
Human
UFormimidoyltransferase-cyclodeaminase
cofactor
Human
UAspartate aminotransferase, mitochondrial
cofactor
Human
UGlycogen phosphorylase, brain form
cofactor
Human
UGlycogen phosphorylase, muscle form
cofactor
Human
UAromatic-L-amino-acid decarboxylase
cofactor
Human
UAspartate aminotransferase
cofactor
Human
UGAD1 protein
cofactor
Human
USerine hydroxymethyltransferase
cofactor
Human
USelenocysteine lyase variant
cofactor
Human
UPhosphorylase
cofactor
Human
UOrnithine aminotransferase variant
cofactor
Human
U5-aminolevulinate synthase
cofactor
Human
UGlutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa)
cofactor
Human
UDDC protein
cofactor
Human
UPyridoxal-dependent decarboxylase domain-containing protein 1
cofactor
Human
UKynurenine--oxoglutarate transaminase 3
cofactor
Human
UGlutamate decarboxylase-like protein 1
cofactor
Human
USelenocysteine lyase
cofactor
Human
UImmunoglobulin superfamily member 10
cofactor
Human
U5-phosphohydroxy-L-lysine phospho-lyase
cofactor
Human
UGlutamate decarboxylase 1 (Brain, 67kDa)
cofactor
Human
USerine hydroxymethyltransferase, mitochondrial
cofactor
Human
U5-aminolevulinate synthase, erythroid-specific, mitochondrial
cofactor
Human
UAlanine aminotransferase 2
cofactor
Human
UMolybdenum cofactor sulfurase
cofactor
Human
USerine dehydratase-like
cofactor
Human
UP-selectin cytoplasmic tail-associated protein (PCAP)
cofactor
Human
UHepatic peroxysomal alanine:glyoxylate aminotransferase
cofactor
Human
USerine racemase
cofactor
Human
UO-phosphoseryl-tRNA(Sec) selenium transferase
cofactor
Human
USerine palmitoyltransferase 3
cofactor
Human
UGlutamic acid decarboxylase
cofactor
Human
UAlanine-glyoxylate aminotransferase homolog
cofactor
Human
Absorption
Not Available
Volume of distribution
Not Available
Protein binding
Not Available
Metabolism
Not Available
Route of elimination
Not Available
Half life
Not Available
Clearance
Not Available
Toxicity
Not Available
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategory
Beta-Alanine MetabolismMetabolic
Catecholamine BiosynthesisMetabolic
Cysteine MetabolismMetabolic
Malate-Aspartate ShuttleMetabolic
Cystathionine Beta-Synthase DeficiencyDisease
Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)Disease
3-Methylcrotonyl Coa Carboxylase Deficiency Type IDisease
Saccharopinuria/Hyperlysinemia IIDisease
Congenital Erythropoietic Porphyria (CEP) or Gunther DiseaseDisease
Porphyria Variegata (PV)Disease
Gaucher DiseaseDisease
Pyruvate Carboxylase DeficiencyDisease
Hyperprolinemia Type IIDisease
Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)Disease
Tyrosinemia Type 2 (or Richner-Hanhart syndrome)Disease
Tyrosinemia Type 3 (TYRO3)Disease
HypophosphatasiaDisease
Creatine deficiency, guanidinoacetate methyltransferase deficiencyDisease
Hyperornithinemia with gyrate atrophy (HOGA)Disease
Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]Disease
L-arginine:glycine amidinotransferase deficiencyDisease
Sucrase-isomaltase deficiencyDisease
Succinic semialdehyde dehydrogenase deficiencyDisease
3-Phosphoglycerate dehydrogenase deficiencyDisease
Cystinosis, ocular nonnephropathicDisease
Argininosuccinic AciduriaDisease
Tyrosine MetabolismMetabolic
Propanoate MetabolismMetabolic
Taurine and Hypotaurine MetabolismMetabolic
Valine, Leucine and Isoleucine DegradationMetabolic
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
Not Available
Food Interactions
Not Available

References

Synthesis Reference

Robert C. Siegel, "Synthesis of cross-links in the helical domain of collagen using pyridoxal 5-phosphate and copper or iron." U.S. Patent US4544638, issued June, 1981.

US4544638
General References
Not Available
External Links
Human Metabolome Database
HMDB01491
KEGG Drug
D00006
KEGG Compound
C00018
PubChem Compound
1051
PubChem Substance
46506428
ChemSpider
1022
BindingDB
50118216
ChEBI
18405
ChEMBL
CHEMBL82202
Therapeutic Targets Database
DNC001499
PharmGKB
PA164749650
HET
PLP
PDRhealth
PDRhealth Drug Page
Wikipedia
Pyridoxal-phosphate
ATC Codes
A11HA06 — Pyridoxal phosphate
PDB Entries
1a3g / 1a50 / 1a5a / 1a5b / 1a5s / 1aam / 1aaw / 1ahe / 1ahf / 1ahg
show 894 more
MSDS
Download (36.1 KB)

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
2TerminatedTreatmentTardive Dyskinesia1

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Dosage forms
FormRouteStrength
Capsule, delayed release pelletsOral
Prices
Not Available
Patents
Not Available

Properties

State
Solid
Experimental Properties
PropertyValueSource
melting point (°C)255 °CPhysProp
water solubilityAppreciableNot Available
logP-1.2Not Available
Predicted Properties
PropertyValueSource
Water Solubility5.7 mg/mLALOGPS
logP-0.55ALOGPS
logP-2.1ChemAxon
logS-1.6ALOGPS
pKa (Strongest Acidic)1.68ChemAxon
pKa (Strongest Basic)4.11ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count6ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area116.95 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity54.75 m3·mol-1ChemAxon
Polarizability20.9 Å3ChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted ADMET features
PropertyValueProbability
Human Intestinal Absorption+0.5078
Blood Brain Barrier+0.8022
Caco-2 permeable-0.6476
P-glycoprotein substrateNon-substrate0.6324
P-glycoprotein inhibitor INon-inhibitor0.9035
P-glycoprotein inhibitor IINon-inhibitor0.9694
Renal organic cation transporterNon-inhibitor0.882
CYP450 2C9 substrateNon-substrate0.6828
CYP450 2D6 substrateNon-substrate0.7978
CYP450 3A4 substrateNon-substrate0.5915
CYP450 1A2 substrateNon-inhibitor0.8704
CYP450 2C9 inhibitorNon-inhibitor0.9041
CYP450 2D6 inhibitorNon-inhibitor0.901
CYP450 2C19 inhibitorNon-inhibitor0.8772
CYP450 3A4 inhibitorNon-inhibitor0.9308
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity0.9352
Ames testNon AMES toxic0.6624
CarcinogenicityNon-carcinogens0.8948
BiodegradationReady biodegradable0.5443
Rat acute toxicity1.6531 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.8729
hERG inhibition (predictor II)Non-inhibitor0.9128
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Not Available
Spectra
SpectrumSpectrum TypeSplash Key
GC-MS Spectrum - GC-MS (1 MEOX; 3 TMS)GC-MSsplash10-0gb9-2690000000-c9bacb7e657461e28407
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSNot Available
GC-MS Spectrum - GC-MSGC-MSsplash10-0gb9-2690000000-c9bacb7e657461e28407
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-004j-0910000000-0408f3957221fc9882cd
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0gb9-1790000000-b01115fa8b4cfd3612c7
MS/MS Spectrum - Quattro_QQQ 10V, PositiveLC-MS/MSsplash10-0f6t-0690000000-4aa57f3f28f0bdef9dcf
MS/MS Spectrum - Quattro_QQQ 25V, PositiveLC-MS/MSsplash10-0fxx-8900000000-ee972556340c61650528
MS/MS Spectrum - Quattro_QQQ 40V, PositiveLC-MS/MSsplash10-014l-9100000000-3cc29fb51820adecd59c
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, NegativeLC-MS/MSsplash10-0002-0090000000-9b86e80a9dd0de14ab59
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, NegativeLC-MS/MSsplash10-03dj-9800000000-9313aa9cbf19bc6311c5
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, NegativeLC-MS/MSsplash10-0002-9500000000-7ce120a58879e2214ce5
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, NegativeLC-MS/MSsplash10-004j-9200000000-7e6bd8c298613e59fb5d
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, NegativeLC-MS/MSsplash10-004i-9000000000-4c05178b1645bf01f3fa
LC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , PositiveLC-MS/MSsplash10-0udi-3920000000-6c5e6106f5658d1d6c50
LC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , PositiveLC-MS/MSsplash10-0udi-3920000000-f96097815e6922356131
LC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , NegativeLC-MS/MSsplash10-002b-9000000000-2c4e243699a95e3a0f88
LC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , NegativeLC-MS/MSsplash10-002b-9000000000-8aa111485891af9f0d02
Predicted MS/MS Spectrum - 10V, Positive (Annotated)Predicted LC-MS/MSsplash10-0f6t-1790000000-1dcb07cd1110c71f7005
Predicted MS/MS Spectrum - 20V, Positive (Annotated)Predicted LC-MS/MSsplash10-0udi-0900000000-ca6aab7f31a36863a417
Predicted MS/MS Spectrum - 40V, Positive (Annotated)Predicted LC-MS/MSsplash10-0udi-9800000000-053802b9c0533d7943ea
Predicted MS/MS Spectrum - 10V, Negative (Annotated)Predicted LC-MS/MSsplash10-0002-9080000000-12ca63d34d39d59f6b42
Predicted MS/MS Spectrum - 20V, Negative (Annotated)Predicted LC-MS/MSsplash10-004i-9000000000-144099ec201adbbc4684
Predicted MS/MS Spectrum - 40V, Negative (Annotated)Predicted LC-MS/MSsplash10-004i-9000000000-70a9559d65e78c488e7e
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-0002-0090000000-9b86e80a9dd0de14ab59
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-03dj-9800000000-9313aa9cbf19bc6311c5
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-0002-9500000000-7ce120a58879e2214ce5
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-004j-9200000000-7e6bd8c298613e59fb5d
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-004i-9000000000-4c05178b1645bf01f3fa
LC-MS/MS Spectrum - LC-ESI-QTOF , negativeLC-MS/MSsplash10-002b-9000000000-2c4e243699a95e3a0f88
LC-MS/MS Spectrum - LC-ESI-QTOF , negativeLC-MS/MSsplash10-002b-9000000000-8aa111485891af9f0d02
LC-MS/MS Spectrum - LC-ESI-QTOF , positiveLC-MS/MSsplash10-0udi-3920000000-6c5e6106f5658d1d6c50
LC-MS/MS Spectrum - LC-ESI-QTOF , positiveLC-MS/MSsplash10-0udi-3920000000-f96097815e6922356131
1H NMR Spectrum1D NMRNot Applicable
1H NMR Spectrum1D NMRNot Applicable
13C NMR Spectrum1D NMRNot Applicable
[1H,1H] 2D NMR Spectrum2D NMRNot Applicable
[1H,13C] 2D NMR Spectrum2D NMRNot Applicable

Taxonomy

Description
This compound belongs to the class of organic compounds known as pyridoxals and derivatives. These are compounds containing a pyridoxal moiety, which consists of a pyridine ring substituted at positions 2,3,4, and 5 by a methyl group, a hydroxyl group, a carbaldehyde group, and a hydroxymethyl group, respectively.
Kingdom
Organic compounds
Super Class
Organoheterocyclic compounds
Class
Pyridines and derivatives
Sub Class
Pyridine carboxaldehydes
Direct Parent
Pyridoxals and derivatives
Alternative Parents
Monoalkyl phosphates / Methylpyridines / Hydroxypyridines / Aryl-aldehydes / Vinylogous acids / Heteroaromatic compounds / Azacyclic compounds / Organopnictogen compounds / Organonitrogen compounds / Organic oxides
show 1 more
Substituents
Pyridoxal / Aryl-aldehyde / Monoalkyl phosphate / Hydroxypyridine / Methylpyridine / Organic phosphoric acid derivative / Phosphoric acid ester / Alkyl phosphate / Vinylogous acid / Heteroaromatic compound
show 10 more
Molecular Framework
Aromatic heteromonocyclic compounds
External Descriptors
monohydroxypyridine, pyridinecarbaldehyde, methylpyridines, vitamin B6 phosphate (CHEBI:18405)

Targets

Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and th...
Gene Name
AGXT2
Uniprot ID
Q9BYV1
Uniprot Name
Alanine--glyoxylate aminotransferase 2, mitochondrial
Molecular Weight
57155.905 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Lee IS, Muragaki Y, Ideguchi T, Hase T, Tsuji M, Ooshima A, Okuno E, Kido R: Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney. J Biochem. 1995 Apr;117(4):856-62. [PubMed:7592550]
  4. Takada Y, Mori T, Noguchi T: The effect of vitamin B6 deficiency on alanine: glyoxylate aminotransferase isoenzymes in rat liver. Arch Biochem Biophys. 1984 Feb 15;229(1):1-6. [PubMed:6703688]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the production of GABA.
Gene Name
GAD1
Uniprot ID
Q99259
Uniprot Name
Glutamate decarboxylase 1
Molecular Weight
66896.065 Da
References
  1. Hwang IK, Yoo KY, Kim DS, Eum WS, Park JK, Park J, Kwon OS, Kang TC, Choi SY, Won MH: Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia. Neuroscience. 2004;128(3):511-8. [PubMed:15381280]
  2. Rust E, Martin DL, Chen CH: Cofactor and tryptophan accessibility and unfolding of brain glutamate decarboxylase. Arch Biochem Biophys. 2001 Aug 15;392(2):333-40. [PubMed:11488610]
  3. Jin H, Sha D, Wei J, Davis KM, Wu H, Jin Y, Wu JY: Effect of apocalmodulin on recombinant human brain glutamic acid decarboxylase. J Neurochem. 2005 Feb;92(4):739-48. [PubMed:15686475]
  4. Chen CH, Battaglioli G, Martin DL, Hobart SA, Colon W: Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase. Biochim Biophys Acta. 2003 Jan 31;1645(1):63-71. [PubMed:12535612]
  5. Tong JC, Mackay IR, Chin J, Law RH, Fayad K, Rowley MJ: Enzymatic characterization of a recombinant isoform hybrid of glutamic acid decarboxylase (rGAD67/65) expressed in yeast. J Biotechnol. 2002 Aug 7;97(2):183-90. [PubMed:12067524]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Ubiquitin protein ligase binding
Specific Function
Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, th...
Gene Name
CBS
Uniprot ID
P35520
Uniprot Name
Cystathionine beta-synthase
Molecular Weight
60586.05 Da
References
  1. Taoka S, Banerjee R: Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine beta-synthase. J Biol Chem. 2002 Jun 21;277(25):22421-5. Epub 2002 Apr 10. [PubMed:11948191]
  2. Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed:12173932]
  3. Mino K, Ishikawa K: Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J Bacteriol. 2003 Apr;185(7):2277-84. [PubMed:12644499]
  4. Evande R, Ojha S, Banerjee R: Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base. Arch Biochem Biophys. 2004 Jul 15;427(2):188-96. [PubMed:15196993]
  5. Linnebank M, Janosik M, Kozich V, Pronicka E, Kubalska J, Sokolova J, Linnebank A, Schmidt E, Leyendecker C, Klockgether T, Kraus JP, Koch HG: The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central Europe: Vitamin B6 nonresponsiveness and a common ancestral haplotype. Hum Mutat. 2004 Oct;24(4):352-3. [PubMed:15365998]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hyd...
Gene Name
KYNU
Uniprot ID
Q16719
Uniprot Name
Kynureninase
Molecular Weight
52351.14 Da
References
  1. Momany C, Levdikov V, Blagova L, Lima S, Phillips RS: Three-dimensional structure of kynureninase from Pseudomonas fluorescens. Biochemistry. 2004 Feb 10;43(5):1193-203. [PubMed:14756555]
  2. Rooseboom M, Vermeulen NP, Groot EJ, Commandeur JN: Tissue distribution of cytosolic beta-elimination reactions of selenocysteine Se-conjugates in rat and human. Chem Biol Interact. 2002 Aug 15;140(3):243-64. [PubMed:12204580]
  3. Lima S, Khristoforov R, Momany C, Phillips RS: Crystal structure of Homo sapiens kynureninase. Biochemistry. 2007 Mar 13;46(10):2735-44. Epub 2007 Feb 15. [PubMed:17300176]
  4. Walsh HA, Botting NP: Purification and biochemical characterization of some of the properties of recombinant human kynureninase. Eur J Biochem. 2002 Apr;269(8):2069-74. [PubMed:11985583]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Serine binding
Specific Function
Interconversion of serine and glycine.
Gene Name
SHMT1
Uniprot ID
P34896
Uniprot Name
Serine hydroxymethyltransferase, cytosolic
Molecular Weight
53082.18 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Trakatellis A, Dimitriadou A, Exindari M, Christodoulou D, Malissiovas N, Antoniadis A, Haitoglou K: Effect of combination of deoxypyridoxine with known anti-proliferative or immunosuppressive agents on lymphocyte serine hydroxymethyltransferase. Postgrad Med J. 1994;70 Suppl 1:S89-92. [PubMed:7526359]
  4. Jagath JR, Sharma B, Rao NA, Savithri HS: The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. J Biol Chem. 1997 Sep 26;272(39):24355-62. [PubMed:9305893]
  5. Bourguignon J, Neuburger M, Douce R: Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase. Biochem J. 1988 Oct 1;255(1):169-78. [PubMed:3143355]
  6. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofac...
Gene Name
NFS1
Uniprot ID
Q9Y697
Uniprot Name
Cysteine desulfurase, mitochondrial
Molecular Weight
50195.21 Da
References
  1. Ollagnier-De-Choudens S, Mulliez E, Hewitson KS, Fontecave M: Biotin synthase is a pyridoxal phosphate-dependent cysteine desulfurase. Biochemistry. 2002 Jul 23;41(29):9145-52. [PubMed:12119030]
  2. You D, Wang L, Yao F, Zhou X, Deng Z: A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans. Biochemistry. 2007 May 22;46(20):6126-33. Epub 2007 May 1. [PubMed:17469805]
  3. Forlani F, Cereda A, Freuer A, Nimtz M, Leimkuhler S, Pagani S: The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form. FEBS Lett. 2005 Dec 19;579(30):6786-90. Epub 2005 Nov 21. [PubMed:16310786]
  4. Cupp-Vickery JR, Urbina H, Vickery LE: Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J Mol Biol. 2003 Jul 25;330(5):1049-59. [PubMed:12860127]
  5. Frazzon J, Fick JR, Dean DR: Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem Soc Trans. 2002 Aug;30(4):680-5. [PubMed:12196163]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Activator
General Function
Pyridoxal phosphate binding
Specific Function
Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a sca...
Gene Name
GOT1
Uniprot ID
P17174
Uniprot Name
Aspartate aminotransferase, cytoplasmic
Molecular Weight
46247.14 Da
References
  1. Hansen CM, Shultz TD: Stability of vitamin B-6-dependent aminotransferase activity in frozen packed erythrocytes is dependent on storage temperature. J Nutr. 2001 May;131(5):1581-3. [PubMed:11340119]
  2. Eliot AC, Kirsch JF: Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. Biochemistry. 2002 Mar 19;41(11):3836-42. [PubMed:11888303]
  3. Cooper AJ, Bruschi SA, Anders MW: Toxic, halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism. Biochem Pharmacol. 2002 Aug 15;64(4):553-64. [PubMed:12167474]
  4. Waldmann A, Dorr B, Koschizke JW, Leitzmann C, Hahn A: Dietary intake of vitamin B6 and concentration of vitamin B6 in blood samples of German vegans. Public Health Nutr. 2006 Sep;9(6):779-84. [PubMed:16925884]
  5. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
OAT
Uniprot ID
P04181
Uniprot Name
Ornithine aminotransferase, mitochondrial
Molecular Weight
48534.39 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Protein homodimerization activity
Specific Function
Key enzyme of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine.
Gene Name
ODC1
Uniprot ID
P11926
Uniprot Name
Ornithine decarboxylase
Molecular Weight
51147.73 Da
References
  1. Jackson LK, Goldsmith EJ, Phillips MA: X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibility. J Biol Chem. 2003 Jun 13;278(24):22037-43. Epub 2003 Apr 2. [PubMed:12672797]
  2. Jackson LK, Brooks HB, Myers DP, Phillips MA: Ornithine decarboxylase promotes catalysis by binding the carboxylate in a buried pocket containing phenylalanine 397. Biochemistry. 2003 Mar 18;42(10):2933-40. [PubMed:12627959]
  3. Jackson LK, Baldwin J, Akella R, Goldsmith EJ, Phillips MA: Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase. Biochemistry. 2004 Oct 19;43(41):12990-9. [PubMed:15476392]
  4. Khomutov AR: Inhibition of enzymes of polyamine biosynthesis by substrate-like O-substituted hydroxylamines. Biochemistry (Mosc). 2002 Oct;67(10):1159-67. [PubMed:12460114]
  5. Myers DP, Jackson LK, Ipe VG, Murphy GE, Phillips MA: Long-range interactions in the dimer interface of ornithine decarboxylase are important for enzyme function. Biochemistry. 2001 Nov 6;40(44):13230-6. [PubMed:11683631]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykyn...
Gene Name
AADAT
Uniprot ID
Q8N5Z0
Uniprot Name
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Molecular Weight
47351.17 Da
References
  1. Goh DL, Patel A, Thomas GH, Salomons GS, Schor DS, Jakobs C, Geraghty MT: Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT). Mol Genet Metab. 2002 Jul;76(3):172-80. [PubMed:12126930]
  2. Cooper AJ: The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants. Neurochem Int. 2004 Jun;44(8):557-77. [PubMed:15016471]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Inhibitor
General Function
Succinate-semialdehyde dehydrogenase binding
Specific Function
Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-al...
Gene Name
ABAT
Uniprot ID
P80404
Uniprot Name
4-aminobutyrate aminotransferase, mitochondrial
Molecular Weight
56438.405 Da
References
  1. Storici P, De Biase D, Bossa F, Bruno S, Mozzarelli A, Peneff C, Silverman RB, Schirmer T: Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin. J Biol Chem. 2004 Jan 2;279(1):363-73. Epub 2003 Oct 8. [PubMed:14534310]
  2. Hwang IK, Yoo KY, Kim do H, Lee BH, Kwon YG, Won MH: Time course of changes in pyridoxal 5'-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage. Exp Neurol. 2007 Jul;206(1):114-25. Epub 2007 Apr 24. [PubMed:17531224]
  3. Sulaiman SA, Suliman FE, Barghouthi S: Kinetic studies on the inhibition of GABA-T by gamma-vinyl GABA and taurine. J Enzyme Inhib Med Chem. 2003 Aug;18(4):297-301. [PubMed:14567543]
  4. Markova M, Peneff C, Hewlins MJ, Schirmer T, John RA: Determinants of substrate specificity in omega-aminotransferases. J Biol Chem. 2005 Oct 28;280(43):36409-16. Epub 2005 Aug 11. [PubMed:16096275]
  5. Liu W, Peterson PE, Langston JA, Jin X, Zhou X, Fisher AJ, Toney MD: Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry. 2005 Mar 1;44(8):2982-92. [PubMed:15723541]
  6. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxamine-phosphate oxidase activity
Specific Function
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Gene Name
PNPO
Uniprot ID
Q9NVS9
Uniprot Name
Pyridoxine-5'-phosphate oxidase
Molecular Weight
29987.79 Da
References
  1. Gospe SM Jr: Pyridoxine-dependent seizures: new genetic and biochemical clues to help with diagnosis and treatment. Curr Opin Neurol. 2006 Apr;19(2):148-53. [PubMed:16538088]
  2. Hwang IK, Kim DW, Jung JY, Yoo KY, Cho JH, Kwon OS, Kang TC, Choi SY, Kim YS, Won MH: Age-dependent changes of pyridoxal phosphate synthesizing enzymes immunoreactivities and activities in the gerbil hippocampal CA1 region. Mech Ageing Dev. 2005 Dec;126(12):1322-30. Epub 2005 Oct 3. [PubMed:16207494]
  3. Pearl PL, Hartka TR, Taylor J: Diagnosis and treatment of neurotransmitter disorders. Curr Treat Options Neurol. 2006 Nov;8(6):441-50. [PubMed:17032564]
  4. Hoffmann GF, Schmitt B, Windfuhr M, Wagner N, Strehl H, Bagci S, Franz AR, Mills PB, Clayton PT, Baumgartner MR, Steinmann B, Bast T, Wolf NI, Zschocke J: Pyridoxal 5'-phosphate may be curative in early-onset epileptic encephalopathy. J Inherit Metab Dis. 2007 Feb;30(1):96-9. Epub 2006 Dec 23. [PubMed:17216302]
  5. Mills PB, Surtees RA, Champion MP, Beesley CE, Dalton N, Scambler PJ, Heales SJ, Briddon A, Scheimberg I, Hoffmann GF, Zschocke J, Clayton PT: Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase. Hum Mol Genet. 2005 Apr 15;14(8):1077-86. Epub 2005 Mar 16. [PubMed:15772097]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Sphinganine-1-phosphate aldolase activity
Specific Function
Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis.
Gene Name
SGPL1
Uniprot ID
O95470
Uniprot Name
Sphingosine-1-phosphate lyase 1
Molecular Weight
63523.265 Da
References
  1. Ikeda M, Kihara A, Igarashi Y: Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5'-phosphate binding domain exposed to the cytosol. Biochem Biophys Res Commun. 2004 Dec 3;325(1):338-43. [PubMed:15522238]
  2. Bobbin RP: PPADS, an ATP antagonist, attenuates the effects of a moderately intense sound on cochlear mechanics. Hear Res. 2001 Jun;156(1-2):10-6. [PubMed:11377878]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has...
Gene Name
TAT
Uniprot ID
P17735
Uniprot Name
Tyrosine aminotransferase
Molecular Weight
50398.895 Da
References
  1. Biagini MR, Tozzi A, Marcucci R, Paniccia R, Fedi S, Milani S, Galli A, Ceni E, Capanni M, Manta R, Abbate R, Surrenti C: Hyperhomocysteinemia and hypercoagulability in primary biliary cirrhosis. World J Gastroenterol. 2006 Mar 14;12(10):1607-12. [PubMed:16570355]
  2. Clayton TA, Lindon JC, Everett JR, Charuel C, Hanton G, Le Net JL, Provost JP, Nicholson JK: Hepatotoxin-induced hypertyrosinemia and its toxicological significance. Arch Toxicol. 2007 Mar;81(3):201-10. Epub 2006 Aug 11. [PubMed:16902803]
  3. Kim SY, An JJ, Kim DW, Choi SH, Lee SH, Hwang SI, Kwon OS, Kang TC, Won MH, Cho SW, Park J, Eum WS, Lee KS, Choi SY: Tat-mediated protein transduction of human brain pyridoxine-5-P oxidase into PC12 cells. J Biochem Mol Biol. 2006 Jan 31;39(1):76-83. [PubMed:16466641]
  4. Shaffer WA, Luong TN, Rothman SC, Kirsch JF: Quantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase. Protein Sci. 2002 Dec;11(12):2848-59. [PubMed:12441383]
  5. Venhorst J, ter Laak AM, Meijer M, van de Wetering I, Commandeur JN, Rooseboom M, Vermeulen NP: Modeling and molecular dynamics of glutamine transaminase K/cysteine conjugate beta-lyase. J Mol Graph Model. 2003 Sep;22(1):55-70. [PubMed:12798391]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transaminase activity
Specific Function
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to ...
Gene Name
CCBL1
Uniprot ID
Q16773
Uniprot Name
Kynurenine--oxoglutarate transaminase 1
Molecular Weight
47874.765 Da
References
  1. Cooper AJ, Bruschi SA, Anders MW: Toxic, halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism. Biochem Pharmacol. 2002 Aug 15;64(4):553-64. [PubMed:12167474]
  2. Mosca M, Croci C, Mostardini M, Breton J, Malyszko J, Avanzi N, Toma S, Benatti L, Gatti S: Tissue expression and translational control of rat kynurenine aminotransferase/glutamine transaminase K mRNAs. Biochim Biophys Acta. 2003 Jul 9;1628(1):1-10. [PubMed:12850267]
  3. Zhang L, Cooper AJ, Krasnikov BF, Xu H, Bubber P, Pinto JT, Gibson GE, Hanigan MH: Cisplatin-induced toxicity is associated with platinum deposition in mouse kidney mitochondria in vivo and with selective inactivation of the alpha-ketoglutarate dehydrogenase complex in LLC-PK1 cells. Biochemistry. 2006 Jul 25;45(29):8959-71. [PubMed:16846239]
  4. Venhorst J, ter Laak AM, Meijer M, van de Wetering I, Commandeur JN, Rooseboom M, Vermeulen NP: Modeling and molecular dynamics of glutamine transaminase K/cysteine conjugate beta-lyase. J Mol Graph Model. 2003 Sep;22(1):55-70. [PubMed:12798391]
  5. Cooper AJ, Pinto JT: Cysteine S-conjugate beta-lyases. Amino Acids. 2006 Feb;30(1):1-15. Epub 2006 Feb 6. [PubMed:16463021]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Threonine synthase activity
Specific Function
Not Available
Gene Name
THNSL1
Uniprot ID
Q8IYQ7
Uniprot Name
Threonine synthase-like 1
Molecular Weight
83069.54 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Vitamin binding
Specific Function
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
Gene Name
PYGL
Uniprot ID
P06737
Uniprot Name
Glycogen phosphorylase, liver form
Molecular Weight
97147.82 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Beauchamp NJ, Taybert J, Champion MP, Layet V, Heinz-Erian P, Dalton A, Tanner MS, Pronicka E, Sharrard MJ: High frequency of missense mutations in glycogen storage disease type VI. J Inherit Metab Dis. 2007 Oct;30(5):722-34. Epub 2007 Aug 21. [PubMed:17705025]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Serine c-palmitoyltransferase activity
Specific Function
Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate ...
Gene Name
SPTLC2
Uniprot ID
O15270
Uniprot Name
Serine palmitoyltransferase 2
Molecular Weight
62923.765 Da
References
  1. Hanada K: Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. [PubMed:12782147]
  2. Tamura K, Mitsuhashi N, Hara-Nishimura I, Imai H: Characterization of an Arabidopsis cDNA encoding a subunit of serine palmitoyltransferase, the initial enzyme in sphingolipid biosynthesis. Plant Cell Physiol. 2001 Nov;42(11):1274-81. [PubMed:11726713]
  3. Gable K, Han G, Monaghan E, Bacikova D, Natarajan M, Williams R, Dunn TM: Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. J Biol Chem. 2002 Mar 22;277(12):10194-200. Epub 2002 Jan 7. [PubMed:11781309]
  4. Ikushiro H, Hayashi H, Kagamiyama H: A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction. J Biol Chem. 2001 May 25;276(21):18249-56. Epub 2001 Mar 12. [PubMed:11279212]
  5. Tamura K, Nishiura H, Mori J, Imai H: Cloning and characterization of a cDNA encoding serine palmitoyltransferase in Arabidopsis thaliana. Biochem Soc Trans. 2000 Dec;28(6):745-7. [PubMed:11171191]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Sulfinoalanine decarboxylase activity
Specific Function
Not Available
Gene Name
CSAD
Uniprot ID
Q9Y600
Uniprot Name
Cysteine sulfinic acid decarboxylase
Molecular Weight
55022.79 Da
References
  1. Skoldberg F, Rorsman F, Perheentupa J, Landin-Olsson M, Husebye ES, Gustafsson J, Kampe O: Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease. J Clin Endocrinol Metab. 2004 Apr;89(4):1636-40. [PubMed:15070923]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the biosynthesis of histamine from histidine.
Gene Name
HDC
Uniprot ID
P19113
Uniprot Name
Histidine decarboxylase
Molecular Weight
74139.825 Da
References
  1. Skoldberg F, Portela-Gomes GM, Grimelius L, Nilsson G, Perheentupa J, Betterle C, Husebye ES, Gustafsson J, Ronnblom A, Rorsman F, Kampe O: Histidine decarboxylase, a pyridoxal phosphate-dependent enzyme, is an autoantigen of gastric enterochromaffin-like cells. J Clin Endocrinol Metab. 2003 Apr;88(4):1445-52. [PubMed:12679420]
  2. Moya-Garcia AA, Pino-Angeles A, Sanchez-Jimenez F: New structural insights to help in the search for selective inhibitors of mammalian pyridoxal 5'-phosphate-dependent histidine decarboxylase . 4. Synthesis, metabolism and release of histamine. Inflamm Res. 2006 Apr;55 Suppl 1:S55-6. [PubMed:16547811]
  3. Landete JM, Pardo I, Ferrer S: Histamine, histidine, and growth-phase mediated regulation of the histidine decarboxylase gene in lactic acid bacteria isolated from wine. FEMS Microbiol Lett. 2006 Jul;260(1):84-90. [PubMed:16790022]
  4. Skoldberg F, Rorsman F, Perheentupa J, Landin-Olsson M, Husebye ES, Gustafsson J, Kampe O: Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease. J Clin Endocrinol Metab. 2004 Apr;89(4):1636-40. [PubMed:15070923]
  5. Graham DE, Xu H, White RH: Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem. 2002 Jun 28;277(26):23500-7. Epub 2002 Apr 29. [PubMed:11980912]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Putrescine transmembrane transporter activity
Specific Function
Antizyme inhibitor protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake by counteracting the negative effect of antizymes OAZ1, OAZ2 and OAZ3 on ODC1 activi...
Gene Name
AZIN2
Uniprot ID
Q96A70
Uniprot Name
Antizyme inhibitor 2
Molecular Weight
49979.185 Da
References
  1. Graham DE, Xu H, White RH: Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem. 2002 Jun 28;277(26):23500-7. Epub 2002 Apr 29. [PubMed:11980912]
  2. Patel CN, Adcock RS, Sell KG, Oliveira MA: Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2396-8. Epub 2004 Nov 26. [PubMed:15583399]
  3. Kidron H, Repo S, Johnson MS, Salminen TA: Functional classification of amino acid decarboxylases from the alanine racemase structural family by phylogenetic studies. Mol Biol Evol. 2007 Jan;24(1):79-89. Epub 2006 Sep 22. [PubMed:16997906]
  4. Arena ME, Manca de Nadra MC: Biogenic amine production by Lactobacillus. J Appl Microbiol. 2001 Feb;90(2):158-62. [PubMed:11168717]
  5. Shah R, Akella R, Goldsmith EJ, Phillips MA: X-ray structure of Paramecium bursaria Chlorella virus arginine decarboxylase: insight into the structural basis for substrate specificity. Biochemistry. 2007 Mar 13;46(10):2831-41. Epub 2007 Feb 17. [PubMed:17305368]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
SDS
Uniprot ID
P20132
Uniprot Name
L-serine dehydratase/L-threonine deaminase
Molecular Weight
34625.105 Da
References
  1. Sun L, Bartlam M, Liu Y, Pang H, Rao Z: Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver. Protein Sci. 2005 Mar;14(3):791-8. Epub 2005 Feb 2. [PubMed:15689518]
  2. Yamada T, Komoto J, Takata Y, Ogawa H, Pitot HC, Takusagawa F: Crystal structure of serine dehydratase from rat liver. Biochemistry. 2003 Nov 11;42(44):12854-65. [PubMed:14596599]
  3. Sun L, Li X, Dong Y, Yang M, Liu Y, Han X, Zhang X, Pang H, Rao Z: Crystallization and preliminary crystallographic analysis of human serine dehydratase. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2297-9. Epub 2003 Nov 27. [PubMed:14646100]
  4. Ogawa H, Gomi T, Nishizawa M, Hayakawa Y, Endo S, Hayashi K, Ochiai H, Takusagawa F, Pitot HC, Mori H, Sakurai H, Koizumi K, Saiki I, Oda H, Fujishita T, Miwa T, Maruyama M, Kobayashi M: Enzymatic and biochemical properties of a novel human serine dehydratase isoform. Biochim Biophys Acta. 2006 May;1764(5):961-71. Epub 2006 Mar 20. [PubMed:16580895]
  5. Cicchillo RM, Baker MA, Schnitzer EJ, Newman EB, Krebs C, Booker SJ: Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis. J Biol Chem. 2004 Jul 30;279(31):32418-25. Epub 2004 May 19. [PubMed:15155761]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
GCAT
Uniprot ID
O75600
Uniprot Name
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Molecular Weight
45284.6 Da
References
  1. Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, Cygler M: Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Biochemistry. 2001 May 1;40(17):5151-60. [PubMed:11318637]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Lyase activity
Specific Function
The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the rem...
Gene Name
GLDC
Uniprot ID
P23378
Uniprot Name
Glycine dehydrogenase (decarboxylating), mitochondrial
Molecular Weight
112728.805 Da
References
  1. Nakai T, Nakagawa N, Maoka N, Masui R, Kuramitsu S, Kamiya N: Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia. EMBO J. 2005 Apr 20;24(8):1523-36. Epub 2005 Mar 24. [PubMed:15791207]
  2. Igamberdiev AU, Ivlev AA, Bykova NV, Threlkeld CN, Lea PJ, Gardestrom P: Decarboxylation of glycine contributes to carbon isotope fractionation in photosynthetic organisms. Photosynth Res. 2001;67(3):177-84. [PubMed:16228305]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting wi...
Gene Name
GPT
Uniprot ID
P24298
Uniprot Name
Alanine aminotransferase 1
Molecular Weight
54636.415 Da
References
  1. Cheung PY, Fong CC, Ng KT, Lam WC, Leung YC, Tsang CW, Yang M, Wong MS: Interaction between pyridoxal kinase and pyridoxal-5-phosphate-dependent enzymes. J Biochem. 2003 Nov;134(5):731-8. [PubMed:14688239]
  2. Halfon P, Imbert-Bismut F, Messous D, Antoniotti G, Benchetrit D, Cart-Lamy P, Delaporte G, Doutheau D, Klump T, Sala M, Thibaud D, Trepo E, Thabut D, Myers RP, Poynard T: A prospective assessment of the inter-laboratory variability of biochemical markers of fibrosis (FibroTest) and activity (ActiTest) in patients with chronic liver disease. Comp Hepatol. 2002 Dec 30;1(1):3. [PubMed:12537583]
  3. Inubushi T, Takasawa T, Tuboi Y, Watanabe N, Aki K, Katunuma N: Changes of glucose metabolism and skin-collagen neogenesis in vitamin B6 deficiency. Biofactors. 2005;23(2):59-67. [PubMed:16179747]
  4. Baines CJ, McKeown-Eyssen GE, Riley N, Cole DE, Marshall L, Loescher B, Jazmaji V: Case-control study of multiple chemical sensitivity, comparing haematology, biochemistry, vitamins and serum volatile organic compound measures. Occup Med (Lond). 2004 Sep;54(6):408-18. Epub 2004 Sep 3. [PubMed:15347780]
  5. Beranek M, Drsata J, Palicka V: Inhibitory effect of glycation on catalytic activity of alanine aminotransferase. Mol Cell Biochem. 2001 Feb;218(1-2):35-9. [PubMed:11330835]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
O-phospho-l-serine:2-oxoglutarate aminotransferase activity
Specific Function
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Gene Name
PSAT1
Uniprot ID
Q9Y617
Uniprot Name
Phosphoserine aminotransferase
Molecular Weight
40422.355 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Battchikova N, Himanen JP, Ahjolahti M, Korpela T: Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing. Biochim Biophys Acta. 1996 Jul 18;1295(2):187-94. [PubMed:8695645]
  4. Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN: Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate. J Mol Biol. 1999 Feb 26;286(3):829-50. [PubMed:10024454]
  5. Kapetaniou EG, Thanassoulas A, Dubnovitsky AP, Nounesis G, Papageorgiou AC: Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies. Proteins. 2006 Jun 1;63(4):742-53. [PubMed:16532449]
  6. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
ALAS1
Uniprot ID
P13196
Uniprot Name
5-aminolevulinate synthase, nonspecific, mitochondrial
Molecular Weight
70580.325 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Nakamura I, Isobe N, Nakamura N, Kamihara T, Fukui S: Mechanism of thiamine-induced respiratory deficiency in Saccharomyces carlsbergensis. J Bacteriol. 1981 Sep;147(3):954-61. [PubMed:7275938]
  4. Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T: A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. Am J Hematol. 1999 Oct;62(2):112-4. [PubMed:10577279]
  5. Shoolingin-Jordan PM, Al-Daihan S, Alexeev D, Baxter RL, Bottomley SS, Kahari ID, Roy I, Sarwar M, Sawyer L, Wang SF: 5-Aminolevulinic acid synthase: mechanism, mutations and medicine. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):361-6. [PubMed:12686158]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transaminase activity
Specific Function
Not Available
Gene Name
AGXT
Uniprot ID
P21549
Uniprot Name
Serine--pyruvate aminotransferase
Molecular Weight
43009.535 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Coulter-Mackie MB, Lian Q: Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations. Mol Genet Metab. 2006 Dec;89(4):349-59. Epub 2006 Sep 12. [PubMed:16971151]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphatase activity
Specific Function
Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization...
Gene Name
PDXP
Uniprot ID
Q96GD0
Uniprot Name
Pyridoxal phosphate phosphatase
Molecular Weight
31697.735 Da
References
  1. Jang YM, Kim DW, Kang TC, Won MH, Baek NI, Moon BJ, Choi SY, Kwon OS: Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J Biol Chem. 2003 Dec 12;278(50):50040-6. Epub 2003 Sep 30. [PubMed:14522954]
  2. McCarty MF: Increased homocyst(e)ine associated with smoking, chronic inflammation, and aging may reflect acute-phase induction of pyridoxal phosphatase activity. Med Hypotheses. 2000 Oct;55(4):289-93. [PubMed:11000053]
  3. Hwang IK, Yoo KY, Kim do H, Lee BH, Kwon YG, Won MH: Time course of changes in pyridoxal 5'-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage. Exp Neurol. 2007 Jul;206(1):114-25. Epub 2007 Apr 24. [PubMed:17531224]
  4. Kim DW, Eum WS, Choi HS, Kim SY, An JJ, Lee SH, Sohn EJ, Hwang SI, Kwon OS, Kang TC, Won MH, Cho SW, Lee KS, Park J, Choi SY: Human brain pyridoxal-5'-phosphate phosphatase: production and characterization of monoclonal antibodies. J Biochem Mol Biol. 2005 Nov 30;38(6):703-8. [PubMed:16336786]
  5. Tirrell IM, Wall JL, Daley CJ, Denial SJ, Tennis FG, Galens KG, O'Handley SF: YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily. Biochem J. 2006 Mar 15;394(Pt 3):665-74. [PubMed:16336194]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Serine c-palmitoyltransferase activity
Specific Function
Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the subst...
Gene Name
SPTLC1
Uniprot ID
O15269
Uniprot Name
Serine palmitoyltransferase 1
Molecular Weight
52743.41 Da
References
  1. Hanada K: Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. [PubMed:12782147]
  2. Gable K, Han G, Monaghan E, Bacikova D, Natarajan M, Williams R, Dunn TM: Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. J Biol Chem. 2002 Mar 22;277(12):10194-200. Epub 2002 Jan 7. [PubMed:11781309]
  3. Ikushiro H, Hayashi H, Kagamiyama H: A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction. J Biol Chem. 2001 May 25;276(21):18249-56. Epub 2001 Mar 12. [PubMed:11279212]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two c...
Gene Name
CTH
Uniprot ID
P32929
Uniprot Name
Cystathionine gamma-lyase
Molecular Weight
44507.64 Da
References
  1. Yamagata S, Akamatsu T, Iwama T: Immobilization of Saccharomyces cerevisiae cystathionine gamma-lyase and application of the product to cystathionine synthesis. Appl Environ Microbiol. 2004 Jun;70(6):3766-8. [PubMed:15184188]
  2. Bertoldi M, Cellini B, Laurents DV, Borri Voltattorni C: Folding pathway of the pyridoxal 5'-phosphate C-S lyase MalY from Escherichia coli. Biochem J. 2005 Aug 1;389(Pt 3):885-98. [PubMed:15823094]
  3. Lowicka E, Beltowski J: Hydrogen sulfide (H2S) - the third gas of interest for pharmacologists. Pharmacol Rep. 2007 Jan-Feb;59(1):4-24. [PubMed:17377202]
  4. Lima CP, Davis SR, Mackey AD, Scheer JB, Williamson J, Gregory JF 3rd: Vitamin B-6 deficiency suppresses the hepatic transsulfuration pathway but increases glutathione concentration in rats fed AIN-76A or AIN-93G diets. J Nutr. 2006 Aug;136(8):2141-7. [PubMed:16857832]
  5. Okuno T, Kubota T, Kuroda T, Ueno H, Nakamuro K: Contribution of enzymic alpha, gamma-elimination reaction in detoxification pathway of selenomethionine in mouse liver. Toxicol Appl Pharmacol. 2001 Oct 1;176(1):18-23. [PubMed:11578145]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
L-valine transaminase activity
Specific Function
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Gene Name
BCAT1
Uniprot ID
P54687
Uniprot Name
Branched-chain-amino-acid aminotransferase, cytosolic
Molecular Weight
42965.815 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
L-valine transaminase activity
Specific Function
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
Gene Name
BCAT2
Uniprot ID
O15382
Uniprot Name
Branched-chain-amino-acid aminotransferase, mitochondrial
Molecular Weight
44287.445 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
PROSC
Uniprot ID
O94903
Uniprot Name
Proline synthase co-transcribed bacterial homolog protein
Molecular Weight
30343.7 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Microtubule binding
Specific Function
Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.Binds and promotes bundling of vimentin...
Gene Name
FTCD
Uniprot ID
O95954
Uniprot Name
Formimidoyltransferase-cyclodeaminase
Molecular Weight
58925.93 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange betwe...
Gene Name
GOT2
Uniprot ID
P00505
Uniprot Name
Aspartate aminotransferase, mitochondrial
Molecular Weight
47517.285 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Mavrides C, Orr W: Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli. J Biol Chem. 1975 Jun 10;250(11):4128-33. [PubMed:236311]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
Gene Name
PYGB
Uniprot ID
P11216
Uniprot Name
Glycogen phosphorylase, brain form
Molecular Weight
96695.18 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
Gene Name
PYGM
Uniprot ID
P11217
Uniprot Name
Glycogen phosphorylase, muscle form
Molecular Weight
97091.265 Da
References
  1. Livanova NB, Chebotareva NA, Eronina TB, Kurganov BI: Pyridoxal 5'-phosphate as a catalytic and conformational cofactor of muscle glycogen phosphorylase B. Biochemistry (Mosc). 2002 Oct;67(10):1089-98. [PubMed:12460107]
  2. Kurganov BI, Kornilaev BA, Chebotareva NA, Malikov VP, Orlov VN, Lyubarev AE, Livanova NB: Dissociative mechanism of thermal denaturation of rabbit skeletal muscle glycogen phosphorylase b. Biochemistry. 2000 Oct 31;39(43):13144-52. [PubMed:11052666]
  3. Okada M, Shibuya M, Yamamoto E, Murakami Y: Effect of diabetes on vitamin B6 requirement in experimental animals. Diabetes Obes Metab. 1999 Jul;1(4):221-5. [PubMed:11228757]
  4. Okada M, Goda H, Kondo Y, Murakami Y, Shibuya M: Effect of exercise on the metabolism of vitamin B6 and some PLP-dependent enzymes in young rats fed a restricted vitamin B6 diet. J Nutr Sci Vitaminol (Tokyo). 2001 Apr;47(2):116-21. [PubMed:11508701]
  5. Geremia S, Campagnolo M, Schinzel R, Johnson LN: Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. J Mol Biol. 2002 Sep 13;322(2):413-23. [PubMed:12217700]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
Gene Name
DDC
Uniprot ID
P20711
Uniprot Name
Aromatic-L-amino-acid decarboxylase
Molecular Weight
53925.815 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Rahman MK, Nagatsu T, Sakurai T, Hori S, Abe M, Matsuda M: Effect of pyridoxal phosphate deficiency on aromatic L-amino acid decarboxylase activity with L-DOPA and L-5-hydroxytryptophan as substrates in rats. Jpn J Pharmacol. 1982 Oct;32(5):803-11. [PubMed:6983619]
  4. Rorsman F, Husebye ES, Winqvist O, Bjork E, Karlsson FA, Kampe O: Aromatic-L-amino-acid decarboxylase, a pyridoxal phosphate-dependent enzyme, is a beta-cell autoantigen. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8626-9. [PubMed:7567987]
  5. Bertoldi M, Borri Voltattorni C: Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions. Biochem J. 2000 Dec 1;352 Pt 2:533-8. [PubMed:11085948]
  6. Allen GF, Neergheen V, Oppenheim M, Fitzgerald JC, Footitt E, Hyland K, Clayton PT, Land JM, Heales SJ: Pyridoxal 5'-phosphate deficiency causes a loss of aromatic L-amino acid decarboxylase in patients and human neuroblastoma cells, implications for aromatic L-amino acid decarboxylase and vitamin B(6) deficiency states. J Neurochem. 2010 Jul;114(1):87-96. doi: 10.1111/j.1471-4159.2010.06742.x. Epub 2010 Apr 9. [PubMed:20403077]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
GIG18
Uniprot ID
Q2TU84
Uniprot Name
Aspartate aminotransferase
Molecular Weight
46319.2 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the production of GABA.
Gene Name
GAD1
Uniprot ID
Q99259
Uniprot Name
Glutamate decarboxylase 1
Molecular Weight
66896.065 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Bennett CL, Huynh HM, Chance PF, Glass IA, Gospe SM Jr: Genetic heterogeneity for autosomal recessive pyridoxine-dependent seizures. Neurogenetics. 2005 Sep;6(3):143-9. Epub 2005 Aug 2. [PubMed:16075246]
  4. Vassort C, Riviere M, Bruneau G, Gros F, Thibault J, Levan G, Szpirer J, Szpirer C: Assignment of the rat genes coding for dopa decarboxylase (DDC) and glutamic acid decarboxylases (GAD1 and GAD2). Mamm Genome. 1993;4(4):202-6. [PubMed:8499653]
  5. Cormier-Daire V, Dagoneau N, Nabbout R, Burglen L, Penet C, Soufflet C, Desguerre I, Munnich A, Dulac O: A gene for pyridoxine-dependent epilepsy maps to chromosome 5q31. Am J Hum Genet. 2000 Oct;67(4):991-3. Epub 2000 Sep 7. [PubMed:10978228]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Interconversion of serine and glycine.
Gene Name
Not Available
Uniprot ID
Q53ET4
Uniprot Name
Serine hydroxymethyltransferase
Molecular Weight
55973.345 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Mehta R, Shangari N, O'Brien PJ: Preventing cell death induced by carbonyl stress, oxidative stress or mitochondrial toxins with vitamin B anti-AGE agents. Mol Nutr Food Res. 2008 Mar;52(3):379-85. [PubMed:17918169]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Lyase activity
Specific Function
Not Available
Gene Name
Not Available
Uniprot ID
Q59FK2
Uniprot Name
Selenocysteine lyase variant
Molecular Weight
25484.43 Da
References
  1. Heidenreich T, Wollers S, Mendel RR, Bittner F: Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J Biol Chem. 2005 Feb 11;280(6):4213-8. Epub 2004 Nov 22. [PubMed:15561708]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
Gene Name
Not Available
Uniprot ID
Q59GM9
Uniprot Name
Alpha-1,4 glucan phosphorylase
Molecular Weight
98828.62 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transaminase activity
Specific Function
Not Available
Gene Name
Not Available
Uniprot ID
Q59HE2
Uniprot Name
Ornithine aminotransferase variant
Molecular Weight
30736.21 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
ALAS1
Uniprot ID
Q5JAM2
Uniprot Name
5-aminolevulinate synthase
Molecular Weight
70580.325 Da
References
  1. Ferreira GC, Zhang JS: Mechanism of 5-aminolevulinate synthase and the role of the protein environment in controlling the cofactor chemistry. Cell Mol Biol (Noisy-le-grand). 2002 Dec;48(8):827-33. [PubMed:12699240]
  2. Choi HP, Hong JW, Rhee KH, Sung HC: Cloning, expression, and characterization of 5-aminolevulinic acid synthase from Rhodopseudomonas palustris KUGB306. FEMS Microbiol Lett. 2004 Jul 15;236(2):175-81. [PubMed:15251194]
  3. Zhang J, Ferreira GC: Transient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism. J Biol Chem. 2002 Nov 22;277(47):44660-9. Epub 2002 Aug 20. [PubMed:12191993]
  4. Turbeville TD, Zhang J, Hunter GA, Ferreira GC: Histidine 282 in 5-aminolevulinate synthase affects substrate binding and catalysis. Biochemistry. 2007 May 22;46(20):5972-81. Epub 2007 May 1. [PubMed:17469798]
  5. Zhang J, Cheltsov AV, Ferreira GC: Conversion of 5-aminolevulinate synthase into a more active enzyme by linking the two subunits: spectroscopic and kinetic properties. Protein Sci. 2005 May;14(5):1190-200. [PubMed:15840827]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
GAD2
Uniprot ID
Q5VZ30
Uniprot Name
Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa)
Molecular Weight
65410.77 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Bennett CL, Huynh HM, Chance PF, Glass IA, Gospe SM Jr: Genetic heterogeneity for autosomal recessive pyridoxine-dependent seizures. Neurogenetics. 2005 Sep;6(3):143-9. Epub 2005 Aug 2. [PubMed:16075246]
  4. Vassort C, Riviere M, Bruneau G, Gros F, Thibault J, Levan G, Szpirer J, Szpirer C: Assignment of the rat genes coding for dopa decarboxylase (DDC) and glutamic acid decarboxylases (GAD1 and GAD2). Mamm Genome. 1993;4(4):202-6. [PubMed:8499653]
  5. Cormier-Daire V, Dagoneau N, Nabbout R, Burglen L, Penet C, Soufflet C, Desguerre I, Munnich A, Dulac O: A gene for pyridoxine-dependent epilepsy maps to chromosome 5q31. Am J Hum Genet. 2000 Oct;67(4):991-3. Epub 2000 Sep 7. [PubMed:10978228]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
DDC
Uniprot ID
Q6IBS8
Uniprot Name
DDC protein
Molecular Weight
53879.725 Da
References
  1. Tan EK, Cheah SY, Fook-Chong S, Yew K, Chandran VR, Lum SY, Yi Z: Functional COMT variant predicts response to high dose pyridoxine in Parkinson's disease. Am J Med Genet B Neuropsychiatr Genet. 2005 Aug 5;137B(1):1-4. [PubMed:15965967]
  2. Bertoldi M, Borri Voltattorni C: Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions. Biochem J. 2000 Dec 1;352 Pt 2:533-8. [PubMed:11085948]
  3. Yee RE, Cheng DW, Huang SC, Namavari M, Satyamurthy N, Barrio JR: Blood-brain barrier and neuronal membrane transport of 6-[18F]fluoro-L-DOPA. Biochem Pharmacol. 2001 Nov 15;62(10):1409-15. [PubMed:11709201]
  4. Skoldberg F, Portela-Gomes GM, Grimelius L, Nilsson G, Perheentupa J, Betterle C, Husebye ES, Gustafsson J, Ronnblom A, Rorsman F, Kampe O: Histidine decarboxylase, a pyridoxal phosphate-dependent enzyme, is an autoantigen of gastric enterochromaffin-like cells. J Clin Endocrinol Metab. 2003 Apr;88(4):1445-52. [PubMed:12679420]
  5. Skoldberg F, Rorsman F, Perheentupa J, Landin-Olsson M, Husebye ES, Gustafsson J, Kampe O: Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease. J Clin Endocrinol Metab. 2004 Apr;89(4):1636-40. [PubMed:15070923]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
PDXDC1
Uniprot ID
Q6P996
Uniprot Name
Pyridoxal-dependent decarboxylase domain-containing protein 1
Molecular Weight
86706.135 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)c...
Gene Name
CCBL2
Uniprot ID
Q6YP21
Uniprot Name
Kynurenine--oxoglutarate transaminase 3
Molecular Weight
51399.855 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Sulfinoalanine decarboxylase activity
Specific Function
May catalyze the decarboxylation of aspartate, cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotaurine and taurine, respectively. Does not exhibit any decarboxylation activity toward ...
Gene Name
GADL1
Uniprot ID
Q6ZQY3
Uniprot Name
Acidic amino acid decarboxylase GADL1
Molecular Weight
59245.95 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transferase activity
Specific Function
Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
Gene Name
SCLY
Uniprot ID
Q96I15
Uniprot Name
Selenocysteine lyase
Molecular Weight
48148.45 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Not Available
Specific Function
May be involved in the maintenance of osteochondroprogenitor cells pool.
Gene Name
IGSF10
Uniprot ID
Q6WRI0
Uniprot Name
Immunoglobulin superfamily member 10
Molecular Weight
290835.42 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transaminase activity
Specific Function
Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde.
Gene Name
PHYKPL
Uniprot ID
Q8IUZ5
Uniprot Name
5-phosphohydroxy-L-lysine phospho-lyase
Molecular Weight
49710.245 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
GAD1
Uniprot ID
Q8IVA8
Uniprot Name
Glutamate decarboxylase 1 (Brain, 67kDa)
Molecular Weight
66916.045 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Bennett CL, Huynh HM, Chance PF, Glass IA, Gospe SM Jr: Genetic heterogeneity for autosomal recessive pyridoxine-dependent seizures. Neurogenetics. 2005 Sep;6(3):143-9. Epub 2005 Aug 2. [PubMed:16075246]
  4. Vassort C, Riviere M, Bruneau G, Gros F, Thibault J, Levan G, Szpirer J, Szpirer C: Assignment of the rat genes coding for dopa decarboxylase (DDC) and glutamic acid decarboxylases (GAD1 and GAD2). Mamm Genome. 1993;4(4):202-6. [PubMed:8499653]
  5. Cormier-Daire V, Dagoneau N, Nabbout R, Burglen L, Penet C, Soufflet C, Desguerre I, Munnich A, Dulac O: A gene for pyridoxine-dependent epilepsy maps to chromosome 5q31. Am J Hum Genet. 2000 Oct;67(4):991-3. Epub 2000 Sep 7. [PubMed:10978228]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA.
Gene Name
SHMT2
Uniprot ID
P34897
Uniprot Name
Serine hydroxymethyltransferase, mitochondrial
Molecular Weight
55992.385 Da
References
  1. Bhavani S, Trivedi V, Jala VR, Subramanya HS, Kaul P, Prakash V, Appaji Rao N, Savithri HS: Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase--crystal structure and kinetic studies. Biochemistry. 2005 May 10;44(18):6929-37. [PubMed:15865438]
  2. Trivedi V, Gupta A, Jala VR, Saravanan P, Rao GS, Rao NA, Savithri HS, Subramanya HS: Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism. J Biol Chem. 2002 May 10;277(19):17161-9. Epub 2002 Feb 27. [PubMed:11877399]
  3. Perry C, Yu S, Chen J, Matharu KS, Stover PJ: Effect of vitamin B6 availability on serine hydroxymethyltransferase in MCF-7 cells. Arch Biochem Biophys. 2007 Jun 1;462(1):21-7. Epub 2007 Apr 20. [PubMed:17482557]
  4. Rajaram V, Bhavani BS, Kaul P, Prakash V, Appaji Rao N, Savithri HS, Murthy MR: Structure determination and biochemical studies on Bacillus stearothermophilus E53Q serine hydroxymethyltransferase and its complexes provide insights on function and enzyme memory. FEBS J. 2007 Aug;274(16):4148-60. Epub 2007 Jul 25. [PubMed:17651438]
  5. Mukherjee M, Sievers SA, Brown MT, Johnson PJ: Identification and biochemical characterization of serine hydroxymethyl transferase in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell. 2006 Dec;5(12):2072-8. Epub 2006 Sep 15. [PubMed:16980404]
  6. Trakatellis A, Dimitriadou A, Exindari M, Christodoulou D, Malissiovas N, Antoniadis A, Haitoglou K: Effect of combination of deoxypyridoxine with known anti-proliferative or immunosuppressive agents on lymphocyte serine hydroxymethyltransferase. Postgrad Med J. 1994;70 Suppl 1:S89-92. [PubMed:7526359]
  7. Jagath JR, Sharma B, Rao NA, Savithri HS: The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. J Biol Chem. 1997 Sep 26;272(39):24355-62. [PubMed:9305893]
  8. Bourguignon J, Neuburger M, Douce R: Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase. Biochem J. 1988 Oct 1;255(1):169-78. [PubMed:3143355]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
ALAS2
Uniprot ID
P22557
Uniprot Name
5-aminolevulinate synthase, erythroid-specific, mitochondrial
Molecular Weight
64632.86 Da
References
  1. Shoolingin-Jordan PM, Al-Daihan S, Alexeev D, Baxter RL, Bottomley SS, Kahari ID, Roy I, Sarwar M, Sawyer L, Wang SF: 5-Aminolevulinic acid synthase: mechanism, mutations and medicine. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):361-6. [PubMed:12686158]
  2. Choi HP, Hong JW, Rhee KH, Sung HC: Cloning, expression, and characterization of 5-aminolevulinic acid synthase from Rhodopseudomonas palustris KUGB306. FEMS Microbiol Lett. 2004 Jul 15;236(2):175-81. [PubMed:15251194]
  3. Heller T, Hochstetter V, Basler M, Borck V: [Vitamin B6-sensitive hereditary sideroblastic anemia]. Dtsch Med Wochenschr. 2004 Jan 23;129(4):141-4. [PubMed:14724775]
  4. Clayton PT: B6-responsive disorders: a model of vitamin dependency. J Inherit Metab Dis. 2006 Apr-Jun;29(2-3):317-26. [PubMed:16763894]
  5. Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW: Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. EMBO J. 2005 Sep 21;24(18):3166-77. Epub 2005 Aug 25. [PubMed:16121195]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.
Gene Name
GPT2
Uniprot ID
Q8TD30
Uniprot Name
Alanine aminotransferase 2
Molecular Weight
57903.11 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Welch S: Comparative studies on the human glutamate-pyruvate transaminase phenotypes--GPT 1, GPT 2-1, GPT 2. Humangenetik. 1975 Sep 20;30(3):237-49. [PubMed:241701]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transferase activity
Specific Function
Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and...
Gene Name
MOCOS
Uniprot ID
Q96EN8
Uniprot Name
Molybdenum cofactor sulfurase
Molecular Weight
98118.965 Da
References
  1. Heidenreich T, Wollers S, Mendel RR, Bittner F: Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J Biol Chem. 2005 Feb 11;280(6):4213-8. Epub 2004 Nov 22. [PubMed:15561708]
  2. Mendel RR, Bittner F: Cell biology of molybdenum. Biochim Biophys Acta. 2006 Jul;1763(7):621-35. Epub 2006 May 12. [PubMed:16784786]
  3. Anantharaman V, Aravind L: MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal-sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases. FEMS Microbiol Lett. 2002 Jan 22;207(1):55-61. [PubMed:11886751]
  4. Bittner F, Oreb M, Mendel RR: ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. J Biol Chem. 2001 Nov 2;276(44):40381-4. Epub 2001 Sep 11. [PubMed:11553608]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Has low serine dehydratase and threonine dehydratase activity.
Gene Name
SDSL
Uniprot ID
Q96GA7
Uniprot Name
Serine dehydratase-like
Molecular Weight
34674.01 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
pcap
Uniprot ID
Q96JQ3
Uniprot Name
P-selectin cytoplasmic tail-associated protein (PCAP)
Molecular Weight
29222.465 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transaminase activity
Specific Function
Not Available
Gene Name
Not Available
Uniprot ID
Q9BXA1
Uniprot Name
Hepatic peroxysomal alanine:glyoxylate aminotransferase
Molecular Weight
39774.51 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Threonine racemase activity
Specific Function
Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
Gene Name
SRR
Uniprot ID
Q9GZT4
Uniprot Name
Serine racemase
Molecular Weight
36565.905 Da
References
  1. Hashimoto A, Yoshikawa M: Effect of aminooxyacetic acid on extracellular level of D-serine in rat striatum: an in vivo microdialysis study. Eur J Pharmacol. 2005 Nov 21;525(1-3):91-3. Epub 2005 Nov 14. [PubMed:16289454]
  2. Strisovsky K, Jiraskova J, Mikulova A, Rulisek L, Konvalinka J: Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity. Biochemistry. 2005 Oct 4;44(39):13091-100. [PubMed:16185077]
  3. Schell MJ: The N-methyl D-aspartate receptor glycine site and D-serine metabolism: an evolutionary perspective. Philos Trans R Soc Lond B Biol Sci. 2004 Jun 29;359(1446):943-64. [PubMed:15306409]
  4. Strisovsky K, Jiraskova J, Barinka C, Majer P, Rojas C, Slusher BS, Konvalinka J: Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate. FEBS Lett. 2003 Jan 30;535(1-3):44-8. [PubMed:12560076]
  5. Uo T, Yoshimura T, Nishiyama T, Esaki N: Gene cloning, purification, and characterization of 2,3-diaminopropionate ammonia-lyase from Escherichia coli. Biosci Biotechnol Biochem. 2002 Dec;66(12):2639-44. [PubMed:12596860]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Trna binding
Specific Function
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Gene Name
SEPSECS
Uniprot ID
Q9HD40
Uniprot Name
O-phosphoseryl-tRNA(Sec) selenium transferase
Molecular Weight
55725.69 Da
References
  1. Xu XM, Carlson BA, Mix H, Zhang Y, Saira K, Glass RS, Berry MJ, Gladyshev VN, Hatfield DL: Biosynthesis of selenocysteine on its tRNA in eukaryotes. PLoS Biol. 2007 Jan;5(1):e4. [PubMed:17194211]
  2. Kernebeck T, Lohse AW, Grotzinger J: A bioinformatical approach suggests the function of the autoimmune hepatitis target antigen soluble liver antigen/liver pancreas. Hepatology. 2001 Aug;34(2):230-3. [PubMed:11481605]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Serine c-palmitoyltransferase activity
Specific Function
Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate ...
Gene Name
SPTLC3
Uniprot ID
Q9NUV7
Uniprot Name
Serine palmitoyltransferase 3
Molecular Weight
62049.035 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Gene Name
GAD65
Uniprot ID
Q9UGI5
Uniprot Name
Glutamic acid decarboxylase
Molecular Weight
47343.69 Da
References
  1. Tong JC, Myers MA, Mackay IR, Zimmet PZ, Rowley MJ: The PEVKEK region of the pyridoxal phosphate binding domain of GAD65 expresses a dominant B cell epitope for type 1 diabetes sera. Ann N Y Acad Sci. 2002 Apr;958:182-9. [PubMed:12021103]
  2. Burd L, Stenehjem A, Franceschini LA, Kerbeshian J: A 15-year follow-up of a boy with pyridoxine (vitamin B6)-dependent seizures with autism, breath holding, and severe mental retardation. J Child Neurol. 2000 Nov;15(11):763-5. [PubMed:11108513]
  3. Myers MA, Davies JM, Tong JC, Whisstock J, Scealy M, Mackay IR, Rowley MJ: Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modeling. J Immunol. 2000 Oct 1;165(7):3830-8. [PubMed:11034389]
  4. Gospe SM Jr: Pyridoxine-dependent seizures: new genetic and biochemical clues to help with diagnosis and treatment. Curr Opin Neurol. 2006 Apr;19(2):148-53. [PubMed:16538088]
  5. Hwang IK, Yoo KY, Kim do H, Lee BH, Kwon YG, Won MH: Time course of changes in pyridoxal 5'-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage. Exp Neurol. 2007 Jul;206(1):114-25. Epub 2007 Apr 24. [PubMed:17531224]
Kind
Protein
Organism
Human
Pharmacological action
Unknown
Actions
Cofactor
General Function
Transaminase activity
Specific Function
Not Available
Gene Name
TLH6
Uniprot ID
Q9UJX1
Uniprot Name
Alanine-glyoxylate aminotransferase homolog
Molecular Weight
28429.215 Da
References
  1. Nishijima S, Sugaya K, Morozumi M, Hatano T, Ogawa Y: Hepatic alanine-glyoxylate aminotransferase activity and oxalate metabolism in vitamin B6 deficient rats. J Urol. 2003 Feb;169(2):683-6. [PubMed:12544342]
  2. Gable K, Han G, Monaghan E, Bacikova D, Natarajan M, Williams R, Dunn TM: Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. J Biol Chem. 2002 Mar 22;277(12):10194-200. Epub 2002 Jan 7. [PubMed:11781309]
  3. Nishijima S, Sugaya K, Morozumi M, Hatano T, Ogawa Y: Capillary electrophoresis assay of alanine:glyoxylate aminotransferase activity in rat liver. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Nov 15;780(1):13-9. [PubMed:12383475]
  4. Nishijima S, Sugaya K, Hokama S, Oshiro Y, Uchida A, Morozumi M, Ogawa Y: Effect of vitamin B6 deficiency on glyoxylate metabolism in rats with or without glyoxylate overload. Biomed Res. 2006 Jun;27(3):93-8. [PubMed:16847354]
  5. Danpure CJ, Lumb MJ, Birdsey GM, Zhang X: Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):70-5. [PubMed:12686111]

Drug created on June 13, 2005 07:24 / Updated on October 02, 2017 04:31