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Identification
NameTetrahydrofolic acid
Accession NumberDB00116  (NUTR00056)
Typesmall molecule
Groupsapproved, nutraceutical
Description

Tetrahydrofolic acid is a folic acid derivative. It is produced from dihydrofolic acid by dihydrofolate reductase.
It is converted into 5,10-methylenetetrahydrofolate by serine hydroxymethyltransferase. It is a coenzyme in many reactions, especially in the metabolism of amino acids and nucleic acids. It acts as a donor of a group with one carbon atom. It gets this carbon atom by sequestering formaldehyde produced in other processes.

Structure
Thumb
Synonyms
SynonymLanguageCode
(6S)-TetrahydrofolateNot AvailableNot Available
(6S)-Tetrahydrofolic acidNot AvailableNot Available
(6S)-THFANot AvailableNot Available
5,6,7,8-tetrahydrofolateNot AvailableNot Available
5,6,7,8-tetrahydrofolic acidNot AvailableNot Available
tetrahydrofolateNot AvailableNot Available
Tetrahydrofolic acidNot AvailableNot Available
THFNot AvailableNot Available
SaltsNot Available
Brand namesNot Available
Brand mixturesNot Available
Categories
CAS number135-16-0
WeightAverage: 445.4292
Monoisotopic: 445.170981503
Chemical FormulaC19H23N7O6
InChI KeyMSTNYGQPCMXVAQ-KIYNQFGBSA-N
InChI
InChI=1S/C19H23N7O6/c20-19-25-15-14(17(30)26-19)23-11(8-22-15)7-21-10-3-1-9(2-4-10)16(29)24-12(18(31)32)5-6-13(27)28/h1-4,11-12,21,23H,5-8H2,(H,24,29)(H,27,28)(H,31,32)(H4,20,22,25,26,30)/t11?,12-/m0/s1
IUPAC Name
(2S)-2-[(4-{[(2-amino-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl)methyl]amino}phenyl)formamido]pentanedioic acid
SMILES
NC1=NC(=O)C2=C(NCC(CNC3=CC=C(C=C3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)N2)N1
Mass SpecNot Available
Taxonomy
KingdomOrganic Compounds
SuperclassHeterocyclic Compounds
ClassPteridines and Derivatives
SubclassPterins and Derivatives
Direct parentPteroic Acids and Derivatives
Alternative parentsN-acyl-alpha Amino Acids; Hippuric Acid Derivatives; Benzoyl Derivatives; Amino Fatty Acids; Pyrimidones; Dicarboxylic Acids and Derivatives; Primary Aromatic Amines; Polyols; Secondary Carboxylic Acid Amides; Polyamines; Carboxylic Acids; Secondary Amines; Enolates
Substituentsn-acyl-alpha amino acid or derivative; n-acyl-alpha-amino acid; hippurate; alpha-amino acid or derivative; benzamide; benzoyl; pyrimidone; benzene; dicarboxylic acid derivative; pyrimidine; primary aromatic amine; secondary carboxylic acid amide; carboxamide group; polyol; polyamine; secondary amine; enolate; carboxylic acid; carboxylic acid derivative; primary amine; amine; organonitrogen compound
Classification descriptionThis compound belongs to the pteroic acids and derivatives. These are compounds that are composed of a pterin with a 4-aminobenzoic acid (or derviative) at the 6 position on the pteridine ring.
Pharmacology
IndicationFor nutritional supplementation, also for treating dietary shortage or imbalance.
PharmacodynamicsTetrahydrofolate is the main active metabolite of dietary folate. It is vital as a coenzyme in reactions involving transfers of single carbon groups. Tetrahydrofolate has a role in nucleic and amino acid synthesis. As nucleic and amino acid synthesis is affected by a deficiency of tetrahydrofolate, actively dividing and growing cells tend to be the first affected. Tetrahydrofolate is used to treat topical sprue and megaloblastic and macrocytic anemias, hematologic complications resulting from a deficiency in folic acid.
Mechanism of actionTetrahydrofolate is transported across cells by receptor-mediated endocytosis where it is needed to maintain normal erythropoiesis, synthesize purine and thymidylate nucleic acids, interconvert amino acids, methylate tRNA, and generate and use formate.
AbsorptionNot Available
Volume of distributionNot Available
Protein bindingNot Available
Metabolism
Route of eliminationNot Available
Half lifeNot Available
ClearanceNot Available
ToxicityNot Available
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategorySMPDB ID
3-Phosphoglycerate dehydrogenase deficiencyDiseaseSMP00721
Homocystinuria due to defect of N(5,10)-methylene THF deficiencyDiseaseSMP00543
Azathioprine Action PathwayDrug actionSMP00427
Thioguanine Action PathwayDrug actionSMP00430
Methotrexate Action PathwayDrug actionSMP00432
Mercaptopurine Action PathwayDrug actionSMP00428
Adenine phosphoribosyltransferase deficiency (APRT)DiseaseSMP00535
Adenosine Deaminase DeficiencyDiseaseSMP00144
S-Adenosylhomocysteine (SAH) Hydrolase DeficiencyDiseaseSMP00214
Methionine Adenosyltransferase DeficiencyDiseaseSMP00221
Adenylosuccinate Lyase DeficiencyDiseaseSMP00167
AICA-RibosiduriaDiseaseSMP00168
Ammonia RecyclingMetabolicSMP00009
Glycine and Serine MetabolismMetabolicSMP00004
Homocystinuria-megaloblastic anemia due to defect in cobalamin metabolism, cblG complementation typeDiseaseSMP00570
Cystathionine Beta-Synthase DeficiencyDiseaseSMP00177
Betaine MetabolismMetabolicSMP00123
Molybdenium Cofactor DeficiencyDiseaseSMP00203
Myoadenylate deaminase deficiencyDiseaseSMP00537
Dihydropyrimidine Dehydrogenase Deficiency (DHPD)DiseaseSMP00179
Xanthine Dehydrogenase Deficiency (Xanthinuria)DiseaseSMP00220
Purine Nucleoside Phosphorylase DeficiencyDiseaseSMP00210
Methylenetetrahydrofolate Reductase Deficiency (MTHFRD)DiseaseSMP00340
Dimethylglycine Dehydrogenase DeficiencyDiseaseSMP00242
Glycine N-methyltransferase DeficiencyDiseaseSMP00222
Mitochondrial DNA depletion syndromeDiseaseSMP00536
DimethylglycinuriaDiseaseSMP00484
Folate malabsorption, hereditaryDiseaseSMP00724
Folate MetabolismMetabolicSMP00053
Gout or Kelley-Seegmiller SyndromeDiseaseSMP00365
Histidine MetabolismMetabolicSMP00044
HistidinemiaDiseaseSMP00191
Non Ketotic HyperglycinemiaDiseaseSMP00223
Hyperglycinemia, non-ketoticDiseaseSMP00485
HypermethioninemiaDiseaseSMP00341
Xanthinuria type IDiseaseSMP00512
Xanthinuria type IIDiseaseSMP00513
Lesch-Nyhan Syndrome (LNS)DiseaseSMP00364
Methionine MetabolismMetabolicSMP00033
Purine MetabolismMetabolicSMP00050
SarcosinemiaDiseaseSMP00244
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
ADMET
Predicted ADMET features
Property Value Probability
Human Intestinal Absorption - 0.5181
Blood Brain Barrier - 0.533
Caco-2 permeable - 0.8443
P-glycoprotein substrate Substrate 0.7509
P-glycoprotein inhibitor I Non-inhibitor 0.972
P-glycoprotein inhibitor II Non-inhibitor 0.9966
Renal organic cation transporter Non-inhibitor 0.8752
CYP450 2C9 substrate Non-substrate 0.8058
CYP450 2D6 substrate Non-substrate 0.7984
CYP450 3A4 substrate Non-substrate 0.637
CYP450 1A2 substrate Non-inhibitor 0.9344
CYP450 2C9 substrate Non-inhibitor 0.9265
CYP450 2D6 substrate Non-inhibitor 0.9437
CYP450 2C19 substrate Non-inhibitor 0.9215
CYP450 3A4 substrate Non-inhibitor 0.9161
CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9631
Ames test Non AMES toxic 0.8293
Carcinogenicity Non-carcinogens 0.954
Biodegradation Not ready biodegradable 0.8759
Rat acute toxicity 2.4563 LD50, mol/kg Not applicable
hERG inhibition (predictor I) Weak inhibitor 0.9534
hERG inhibition (predictor II) Non-inhibitor 0.6623
Pharmacoeconomics
ManufacturersNot Available
PackagersNot Available
Dosage formsNot Available
PricesNot Available
PatentsNot Available
Properties
Statesolid
Experimental Properties
PropertyValueSource
logP-2.7Not Available
Predicted Properties
PropertyValueSource
water solubility2.69e-01 g/lALOGPS
logP-0.96ALOGPS
logP-4.2ChemAxon
logS-3.2ALOGPS
pKa (strongest acidic)3.51ChemAxon
pKa (strongest basic)3.58ChemAxon
physiological charge-2ChemAxon
hydrogen acceptor count12ChemAxon
hydrogen donor count8ChemAxon
polar surface area207.27ChemAxon
rotatable bond count9ChemAxon
refractivity121.39ChemAxon
polarizability42.95ChemAxon
number of rings3ChemAxon
bioavailability0ChemAxon
rule of fiveNoChemAxon
Ghose filterNoChemAxon
Veber's ruleNoChemAxon
MDDR-like ruleYesChemAxon
Spectra
SpectraNot Available
References
Synthesis Reference

Attilio Melera, Fabrizio Marazza, “Process for the preparation of alkaline earth metal salts of (6R)-N(10)-formyl-5,6,7,8-tetrahydrofolic acid.” U.S. Patent US5332815, issued May, 1954.

US5332815
General ReferenceNot Available
External Links
ResourceLink
KEGG CompoundC00101
PubChem Compound91443
PubChem Substance46504756
ChemSpider82572
ChEBI20506
ChEMBL
Therapeutic Targets DatabaseDAP001308
PharmGKBPA164745110
HETTHL
WikipediaTetrahydrofolic_acid
ATC CodesNot Available
AHFS CodesNot Available
PDB Entries
FDA labelNot Available
MSDSNot Available
Interactions
Drug InteractionsNot Available
Food InteractionsNot Available

Targets

1. C-1-tetrahydrofolate synthase, cytoplasmic

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
C-1-tetrahydrofolate synthase, cytoplasmic P11586 Details

References:

  1. Akar N, Akar E, Ozel D, Deda G, Sipahi T: Common mutations at the homocysteine metabolism pathway and pediatric stroke. Thromb Res. 2001 Apr 15;102(2):115-20. Pubmed
  2. Walkup AS, Appling DR: Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase. Arch Biochem Biophys. 2005 Oct 15;442(2):196-205. Epub 2005 Aug 30. Pubmed
  3. Matakidou A, El Galta R, Rudd MF, Webb EL, Bridle H, Eisen T, Houlston RS: Prognostic significance of folate metabolism polymorphisms for lung cancer. Br J Cancer. 2007 Jul 16;97(2):247-52. Epub 2007 May 29. Pubmed
  4. Salmassi TM, Leadbetter JR: Analysis of genes of tetrahydrofolate-dependent metabolism from cultivated spirochaetes and the gut community of the termite Zootermopsis angusticollis. Microbiology. 2003 Sep;149(Pt 9):2529-37. Pubmed
  5. Prasannan P, Pike S, Peng K, Shane B, Appling DR: Human mitochondrial C1-tetrahydrofolate synthase: gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary calls. J Biol Chem. 2003 Oct 31;278(44):43178-87. Epub 2003 Aug 22. Pubmed

2. Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial P13995 Details

References:

  1. Salmassi TM, Leadbetter JR: Analysis of genes of tetrahydrofolate-dependent metabolism from cultivated spirochaetes and the gut community of the termite Zootermopsis angusticollis. Microbiology. 2003 Sep;149(Pt 9):2529-37. Pubmed

3. Aminomethyltransferase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Aminomethyltransferase, mitochondrial P48728 Details

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
  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
  3. Masai E, Sasaki M, Minakawa Y, Abe T, Sonoki T, Miyauchi K, Katayama Y, Fukuda M: A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J Bacteriol. 2004 May;186(9):2757-65. Pubmed

4. Cytosolic 10-formyltetrahydrofolate dehydrogenase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Cytosolic 10-formyltetrahydrofolate dehydrogenase O75891 Details

References:

  1. Fu TF, Maras B, Barra D, Schirch V: A noncatalytic tetrahydrofolate tight binding site is on the small domain of 10-formyltetrahydrofolate dehydrogenase. Arch Biochem Biophys. 1999 Jul 15;367(2):161-6. Pubmed
  2. Krupenko SA, Wagner C: Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase. J Biol Chem. 1999 Dec 10;274(50):35777-84. Pubmed
  3. Krupenko SA, Vlasov AP, Wagner C: On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis: connection between hydrolase and dehydrogenase mechanisms. J Biol Chem. 2001 Jun 29;276(26):24030-7. Epub 2001 Apr 24. Pubmed
  4. Anguera MC, Field MS, Perry C, Ghandour H, Chiang EP, Selhub J, Shane B, Stover PJ: Regulation of folate-mediated one-carbon metabolism by 10-formyltetrahydrofolate dehydrogenase. J Biol Chem. 2006 Jul 7;281(27):18335-42. Epub 2006 Apr 20. Pubmed
  5. Oleinik NV, Krupenko NI, Reuland SN, Krupenko SA: Leucovorin-induced resistance against FDH growth suppressor effects occurs through DHFR up-regulation. Biochem Pharmacol. 2006 Jul 14;72(2):256-66. Epub 2006 Apr 25. Pubmed

5. Methionine synthase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Methionine synthase Q99707 Details

References:

  1. Hall DA, Jordan-Starck TC, Loo RO, Ludwig ML, Matthews RG: Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry. 2000 Sep 5;39(35):10711-9. Pubmed
  2. Fowler B: The folate cycle and disease in humans. Kidney Int Suppl. 2001 Feb;78:S221-9. Pubmed
  3. Fu TF, di Salvo M, Schirch V: Enzymatic determination of homocysteine in cell extracts. Anal Biochem. 2001 Mar;290(2):359-65. Pubmed
  4. Jarrett JT, Choi CY, Matthews RG: Changes in protonation associated with substrate binding and Cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry. 1997 Dec 16;36(50):15739-48. Pubmed
  5. Jarrett JT, Hoover DM, Ludwig ML, Matthews RG: The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzyme. Biochemistry. 1998 Sep 8;37(36):12649-58. Pubmed

6. Formimidoyltransferase-cyclodeaminase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Formimidoyltransferase-cyclodeaminase O95954 Details

References:

  1. Bashour AM, Bloom GS: 58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase. J Biol Chem. 1998 Jul 31;273(31):19612-7. Pubmed
  2. Cook RJ: Disruption of histidine catabolism in NEUT2 mice. Arch Biochem Biophys. 2001 Aug 15;392(2):226-32. Pubmed
  3. Kohls D, Croteau N, Mejia N, MacKenzie RE, Vrielink A: Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase. Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1206-8. Pubmed
  4. Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A: The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme. Structure. 2000 Jan 15;8(1):35-46. Pubmed

7. Bifunctional purine biosynthesis protein PURH

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Bifunctional purine biosynthesis protein PURH P31939 Details

References:

  1. Wolan DW, Greasley SE, Wall MJ, Benkovic SJ, Wilson IA: Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site. Biochemistry. 2003 Sep 23;42(37):10904-14. Pubmed
  2. Bulock KG, Beardsley GP, Anderson KS: The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5’-monophosphate cyclohydrolase). A surprising lack of substrate channeling. J Biol Chem. 2002 Jun 21;277(25):22168-74. Epub 2002 Apr 10. Pubmed

8. Serine hydroxymethyltransferase, cytosolic

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Serine hydroxymethyltransferase, cytosolic P34896 Details

References:

  1. Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT: Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate. J Mol Biol. 2000 Feb 11;296(1):155-68. Pubmed
  2. Rao JV, Prakash V, Rao NA, Savithri HS: The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase. Eur J Biochem. 2000 Oct;267(19):5967-76. Pubmed
  3. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. Pubmed
  4. Ravanel S, Cherest H, Jabrin S, Grunwald D, Surdin-Kerjan Y, Douce R, Rebeille F: Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15360-5. Pubmed
  5. Li R, Moore M, King J: Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana. Plant Cell Physiol. 2003 Mar;44(3):233-41. Pubmed
  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

9. Serine hydroxymethyltransferase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Serine hydroxymethyltransferase, mitochondrial P34897 Details

References:

  1. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. Pubmed
  2. Contestabile R, Paiardini A, Pascarella S, di Salvo ML, D’Aguanno S, Bossa F: l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions. Eur J Biochem. 2001 Dec;268(24):6508-25. Pubmed
  3. Li R, Moore M, King J: Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana. Plant Cell Physiol. 2003 Mar;44(3):233-41. Pubmed
  4. Appaji Rao N, Ambili M, Jala VR, Subramanya HS, Savithri HS: Structure-function relationship in serine hydroxymethyltransferase. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):24-9. Pubmed
  5. Angelaccio S, Chiaraluce R, Consalvi V, Buchenau B, Giangiacomo L, Bossa F, Contestabile R: Catalytic and thermodynamic properties of tetrahydromethanopterin-dependent serine hydroxymethyltransferase from Methanococcus jannaschii. J Biol Chem. 2003 Oct 24;278(43):41789-97. Epub 2003 Aug 5. Pubmed

10. Methylenetetrahydrofolate reductase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Methylenetetrahydrofolate reductase P42898 Details

References:

  1. Ubbink JB, Christianson A, Bester MJ, Van Allen MI, Venter PA, Delport R, Blom HJ, van der Merwe A, Potgieter H, Vermaak WJ: Folate status, homocysteine metabolism, and methylene tetrahydrofolate reductase genotype in rural South African blacks with a history of pregnancy complicated by neural tube defects. Metabolism. 1999 Feb;48(2):269-74. Pubmed
  2. Heijmans BT, Gussekloo J, Kluft C, Droog S, Lagaay AM, Knook DL, Westendorp RG, Slagboom EP: Mortality risk in men is associated with a common mutation in the methylene-tetrahydrofolate reductase gene (MTHFR). Eur J Hum Genet. 1999 Feb-Mar;7(2):197-204. Pubmed
  3. Tsai MY, Welge BG, Hanson NQ, Bignell MK, Vessey J, Schwichtenberg K, Yang F, Bullemer FE, Rasmussen R, Graham KJ: Genetic causes of mild hyperhomocysteinemia in patients with premature occlusive coronary artery diseases. Atherosclerosis. 1999 Mar;143(1):163-70. Pubmed
  4. Holmes ZR, Regan L, Chilcott I, Cohen H: The C677T MTHFR gene mutation is not predictive of risk for recurrent fetal loss. Br J Haematol. 1999 Apr;105(1):98-101. Pubmed
  5. Larsson J, Hultberg B, Hillarp A: Hyperhomocysteinemia and the MTHFR C677T mutation in central retinal vein occlusion. Acta Ophthalmol Scand. 2000 Jun;78(3):340-3. Pubmed

11. Serine hydroxymethyltransferase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Serine hydroxymethyltransferase Q53ET4 Details

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
  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
  3. Chang WN, Tsai JN, Chen BH, Huang HS, Fu TF: Serine hydroxymethyltransferase isoforms are differentially inhibited by leucovorin-Characterization and comparison of recombinant zebrafish serine hydroxymethyltransferases. Drug Metab Dispos. 2007 Jul 30;. Pubmed

12. Serine hydroxymethyltransferase, cytosolic

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Serine hydroxymethyltransferase, cytosolic P34896 Details

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
  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

13. Serine hydroxymethyltransferase, cytosolic

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Serine hydroxymethyltransferase, cytosolic P34896 Details

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
  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

14. Methylenetetrahydrofolate reductase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Methylenetetrahydrofolate reductase P42898 Details

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
  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
  3. Siva A, De Lange M, Clayton D, Monteith S, Spector T, Brown MJ: The heritability of plasma homocysteine, and the influence of genetic variation in the homocysteine methylation pathway. QJM. 2007 Aug;100(8):495-9. Epub 2007 Jul 17. Pubmed
  4. Leopardi P, Marcon F, Caiola S, Cafolla A, Siniscalchi E, Zijno A, Crebelli R: Effects of folic acid deficiency and MTHFR C677T polymorphism on spontaneous and radiation-induced micronuclei in human lymphocytes. Mutagenesis. 2006 Sep;21(5):327-33. Epub 2006 Sep 1. Pubmed
  5. Ott K, Vogelsang H, Marton N, Becker K, Lordick F, Kobl M, Schuhmacher C, Novotny A, Mueller J, Fink U, Ulm K, Siewert JR, Hofler H, Keller G: The thymidylate synthase tandem repeat promoter polymorphism: A predictor for tumor-related survival in neoadjuvant treated locally advanced gastric cancer. Int J Cancer. 2006 Dec 15;119(12):2885-94. Pubmed

15. Serine hydroxymethyltransferase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Serine hydroxymethyltransferase, mitochondrial P34897 Details

References:

  1. Prabhu V, Chatson KB, Lui H, Abrams GD, King J: Effects of sulfanilamide and methotrexate on 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in arabidopsis. Plant Physiol. 1998 Jan;116(1):137-44. Pubmed
  2. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. Pubmed
  3. 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
  4. Contestabile R, Paiardini A, Pascarella S, di Salvo ML, D’Aguanno S, Bossa F: l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions. Eur J Biochem. 2001 Dec;268(24):6508-25. Pubmed
  5. Vatsyayan R, Roy U: Molecular cloning and biochemical characterization of Leishmania donovani serine hydroxymethyltransferase. Protein Expr Purif. 2007 Apr;52(2):433-40. Epub 2006 Oct 26. Pubmed

16. Methionyl-tRNA formyltransferase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: cofactor

Components

Name UniProt ID Details
Methionyl-tRNA formyltransferase, mitochondrial Q96DP5 Details

References:

  1. Li Y, Holmes WB, Appling DR, RajBhandary UL: Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA. J Bacteriol. 2000 May;182(10):2886-92. Pubmed

Transporters

1. Canalicular multispecific organic anion transporter 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: inhibitor

Components

Name UniProt ID Details
Canalicular multispecific organic anion transporter 1 Q92887 Details

References:

  1. Kusuhara H, Han YH, Shimoda M, Kokue E, Suzuki H, Sugiyama Y: Reduced folate derivatives are endogenous substrates for cMOAT in rats. Am J Physiol. 1998 Oct;275(4 Pt 1):G789-96. Pubmed

Comments
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Drug created on June 13, 2005 07:24 / Updated on September 16, 2013 17:08