You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on DrugBank.
Identification
NameL-Cysteine
Accession NumberDB00151  (DB04443, NUTR00018)
Typesmall molecule
Groupsapproved, nutraceutical
Description

A thiol-containing non-essential amino acid that is oxidized to form cystine. [PubChem]

Structure
Thumb
Synonyms
SynonymLanguageCode
(2R)-2-amino-3-mercaptopropanoic acidNot AvailableNot Available
(2R)-2-amino-3-sulfanylpropanoic acidNot AvailableNot Available
(R)-2-Amino-3-mercaptopropanoic acidNot AvailableNot Available
CysNot AvailableNot Available
L-2-Amino-3-mercaptopropionic acidNot AvailableNot Available
L-CysNot AvailableNot Available
SaltsNot Available
Brand namesNot Available
Brand mixtures
Brand NameIngredients
Amino Acid Concentrate InjArginine Hcl + Calcium Chloride + Dexpanthenol + Dextrose + Dl-Methionine + Glutamic Acid + Histidine Hcl + Isoleucine + L-Cysteine Hydrochloride + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Nicotinamide + Phenylalanine + Potassium Chloride + Sodium Acetate + Threonine + Tryptophan + Valine + Vitamin B1 (Thiamine) + Vitamin B12 + Vitamin B2 (Riboflavin) + Vitamin B6 (Pyridoxine)
Amino Acid InjArginine + Calcium Chloride + D-Pantothenic Acid (Calcium D-Pantothenate) + Dextrose + Histidine + Isoleucine + L-Cysteine Hydrochloride + Leucine + Lysine + Magnesium Sulfate + Methionine + Nicotinamide + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Acetate + Threonine + Tryptophan + Valine + Vitamin B1 + Vitamin B12 + Vitamin B2
Amino LiteArginine + Calcium Chloride + Dextrose + Isoleucine + L-Cysteine Hydrochloride + L-Histidine Hcl + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Methionine + Nicotinic Acid + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Glutamate + Thiamine Hydrochloride + Threonine + Tryptophan + Valine + Vitamin B12 + Vitamin B2 (Riboflavin 5'-Phosphate Sodium)
Aminoderm PoudreGlycine + L-Cysteine + Neomycin Sulfate + Threonine
Bvs Amino Acid Solution InjArginine Hcl + Calcium Chloride + Dexpanthenol + Dextrose + Dl-Isoleucine + L-Cysteine Hydrochloride + L-Histidine Hcl + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Methionine + Nicotinamide + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Acetate Hemodialysis + Sodium Glutamate + Threonine + Tryptophan + Valine + Vitamin B1 + Vitamin B12 + Vitamin B2
Cicatrin PowderBacitracin Zinc + Glycine + L-Cysteine + Neomycin Sulfate + Threonine
Nephramine Liq IvDl-Methionine + Histidine + Isoleucine + L-Cysteine (L-Cysteine Hydrochloride) + Leucine + Lysine (Lysine Acetate) + Phenylalanine + Sodium Bisulfite + Threonine + Tryptophan + Valine
Primene 10%Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine + L-Isoleucine + L-Leucine + L-Lysine + L-Ornithine Dihydrochloride + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Taurine + Tryptophan
Primene 10%-Liq IvGlutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine Hydrochloride + L-Isoleucine + L-Leucine + L-Lysine + L-Ornithine + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Taurine + Tryptophan
Stv Amino Acid Sol InjArginine Hcl + Calcium Chloride + Dexpanthenol + Dextrose + Dl-Methionine + Glutamic Acid + Histidine Hcl + Isoleucine + L-Cysteine Hydrochloride + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Nicotinamide + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Acetate + Threonine + Tryptophan + Valine + Vitamin B1 (Thiamine) + Vitamin B12 + Vitamin B2 (Riboflavin)
Vamin 18 Electrolyte-FreeGlutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine + L-Isoleucine + L-Leucine + L-Lysine (Lysine Acetate) + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Tryptophan
Vamin NCalcium Chloride + Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine (L-Cysteine Hydrochloride) + L-Isoleucine + L-Leucine + L-Lysine (L-Lysine Hydrochloride) + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Magnesium Sulfate + Methionine + Potassium Chloride + Potassium Hydroxide + Serine + Sodium Hydroxide + Tryptophan
Categories
CAS number52-90-4
WeightAverage: 121.158
Monoisotopic: 121.019749163
Chemical FormulaC3H7NO2S
InChI KeyXUJNEKJLAYXESH-RUOZJJLTNA-N
InChI
InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/s2
IUPAC Name
(2R)-2-amino-3-sulfanylpropanoic acid
SMILES
N[C@@H](CS)C(O)=O
Mass Specshow(8.4 KB)
Taxonomy
KingdomOrganic Compounds
SuperclassOrganic Acids and Derivatives
ClassCarboxylic Acids and Derivatives
SubclassAmino Acids, Peptides, and Analogues
Direct parentAlpha Amino Acids and Derivatives
Alternative parentsPolyamines; Alkylthiols; Carboxylic Acids; Enolates; Monoalkylamines
Substituentsalkylthiol; enolate; carboxylic acid; polyamine; primary amine; amine; primary aliphatic amine; organonitrogen compound
Classification descriptionThis compound belongs to the alpha amino acids and derivatives. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon), or a derivative thereof.
Pharmacology
IndicationFor the prevention of liver damage and kidney damage associated with overdoses of acetaminophen
PharmacodynamicsDue to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine may at some point be recognized as an essential or conditionally essential amino acid.
Mechanism of actionAlthough classified as a non-essential amino acid cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine can usually be synthesized by the human body under normal physiological conditions if a sufficient quantity of methionine is available. Due to the ability of thiols to undergo redox reactions, cysteine has antioxidant properties. Cysteine's antioxidant properties are typically expressed in the tripeptide glutathione, which occurs in humans as well as other organisms. The systemic availability of oral glutathione (GSH) is negligible; so it must be biosynthesized from its constituent amino acids, cysteine, glycine, and glutamic acid. Glutamic acid and glycine are readily available in the diets of most industrialized countries, but the availability of cysteine can be the limiting substrate. Cysteine is also an important source of sulfide in human metabolism. The sulfide in iron-sulfur clusters and in nitrogenase is extracted from cysteine, which is converted to alanine in the process. In a 1994 report released by five top cigarette companies, cysteine is one of the 599 additives to cigarettes. Its use or purpose, however, is unknown, like most cigarette additives. Its inclusion in cigarettes could offer two benefits: Acting as an expectorant, since smoking increases mucus production in the lungs; and increasing the beneficial antioxidant glutathione (which is diminished in smokers).
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
2-Hydroxyglutric Aciduria (D And L Form)DiseaseSMP00136
3-Phosphoglycerate dehydrogenase deficiencyDiseaseSMP00721
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase DeficiencyDiseaseSMP00243
5-oxoprolinase deficiencyDiseaseSMP00500
5-OxoprolinuriaDiseaseSMP00143
Ethacrynic Acid Action PathwayDrug actionSMP00097
Hydrochlorothiazide Action PathwayDrug actionSMP00100
Bendroflumethiazide Action PathwayDrug actionSMP00090
Cyclothiazide Action PathwayDrug actionSMP00103
Quinethazone Action PathwayDrug actionSMP00091
Spironolactone Action PathwayDrug actionSMP00134
Amiloride Action PathwayDrug actionSMP00133
Chlorthalidone Action PathwayDrug actionSMP00122
Hydroflumethiazide Action PathwayDrug actionSMP00108
Torsemide Action PathwayDrug actionSMP00118
Chlorothiazide Action PathwayDrug actionSMP00078
Polythiazide Action PathwayDrug actionSMP00080
Bumetanide Action PathwayDrug actionSMP00088
Furosemide Action PathwayDrug actionSMP00115
Triamterene Action PathwayDrug actionSMP00132
Trichlormethiazide Action PathwayDrug actionSMP00121
Methyclothiazide Action PathwayDrug actionSMP00081
Metolazone Action PathwayDrug actionSMP00105
Indapamide Action PathwayDrug actionSMP00110
Eplerenone Action PathwayDrug actionSMP00135
S-Adenosylhomocysteine (SAH) Hydrolase DeficiencyDiseaseSMP00214
Methionine Adenosyltransferase DeficiencyDiseaseSMP00221
Glycine and Serine MetabolismMetabolicSMP00004
Taurine and Hypotaurine MetabolismMetabolicSMP00021
Pantothenate and CoA BiosynthesisMetabolicSMP00027
Homocystinuria-megaloblastic anemia due to defect in cobalamin metabolism, cblG complementation typeDiseaseSMP00570
Cystathionine Beta-Synthase DeficiencyDiseaseSMP00177
Homocystinuria, cystathionine beta-synthase deficiencyDiseaseSMP00515
Beta-mercaptolactate-cysteine disulfiduriaDiseaseSMP00499
Blue diaper syndromeDiseaseSMP00583
Gamma-cystathionase deficiency (CTH)DiseaseSMP00514
Cysteine MetabolismMetabolicSMP00013
Cystinosis, ocular nonnephropathicDiseaseSMP00722
CystinuriaDiseaseSMP00723
Glucose Transporter Defect (SGLT2)DiseaseSMP00245
Gamma-glutamyl-transpeptidase deficiencyDiseaseSMP00501
Dihydropyrimidine Dehydrogenase Deficiency (DHPD)DiseaseSMP00179
Succinic semialdehyde dehydrogenase deficiencyDiseaseSMP00567
Methylenetetrahydrofolate Reductase Deficiency (MTHFRD)DiseaseSMP00340
Dimethylglycine Dehydrogenase DeficiencyDiseaseSMP00242
Glutathione Synthetase DeficiencyDiseaseSMP00337
Glycine N-methyltransferase DeficiencyDiseaseSMP00222
Gamma-Glutamyltransferase DeficiencyDiseaseSMP00183
Homocysteine DegradationMetabolicSMP00455
DimethylglycinuriaDiseaseSMP00484
Hartnup DisorderDiseaseSMP00189
Kidney FunctionPhysiologicalSMP00483
Renal GlucosuriaDiseaseSMP00184
Glutamate MetabolismMetabolicSMP00072
Glutathione MetabolismMetabolicSMP00015
HomocarnosinosisDiseaseSMP00385
Hyperinsulinism-Hyperammonemia SyndromeDiseaseSMP00339
Non Ketotic HyperglycinemiaDiseaseSMP00223
Hyperglycinemia, non-ketoticDiseaseSMP00485
HypermethioninemiaDiseaseSMP00341
IminoglycinuriaDiseaseSMP00584
IminoglycinuriaDiseaseSMP00193
Lysinuric protein intolerance (LPI)DiseaseSMP00585
Lysinuric Protein IntoleranceDiseaseSMP00197
Methionine MetabolismMetabolicSMP00033
SarcosinemiaDiseaseSMP00244
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
ADMET
Predicted ADMET features
Property Value Probability
Human Intestinal Absorption + 0.9698
Blood Brain Barrier + 0.5918
Caco-2 permeable - 0.721
P-glycoprotein substrate Non-substrate 0.8141
P-glycoprotein inhibitor I Non-inhibitor 0.984
P-glycoprotein inhibitor II Non-inhibitor 0.9903
Renal organic cation transporter Non-inhibitor 0.9462
CYP450 2C9 substrate Non-substrate 0.8473
CYP450 2D6 substrate Non-substrate 0.8141
CYP450 3A4 substrate Non-substrate 0.8245
CYP450 1A2 substrate Non-inhibitor 0.94
CYP450 2C9 substrate Non-inhibitor 0.9584
CYP450 2D6 substrate Non-inhibitor 0.9665
CYP450 2C19 substrate Non-inhibitor 0.9634
CYP450 3A4 substrate Non-inhibitor 0.9602
CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9888
Ames test AMES toxic 0.9107
Carcinogenicity Non-carcinogens 0.7998
Biodegradation Ready biodegradable 0.7577
Rat acute toxicity 1.7757 LD50, mol/kg Not applicable
hERG inhibition (predictor I) Weak inhibitor 0.9891
hERG inhibition (predictor II) Non-inhibitor 0.9684
Pharmacoeconomics
Manufacturers
  • Hospira inc
Packagers
Dosage formsNot Available
Prices
Unit descriptionCostUnit
L-cysteine powder1.65USDg
L-cysteine 50 mg/ml vial0.4USDml
L-cysteine hcl powder0.3USDg
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
PatentsNot Available
Properties
Statesolid
Experimental Properties
PropertyValueSource
melting point240 dec °CPhysProp
water solubility2.77E+005 mg/L (at 25 °C)BEILSTEIN
logP-2.49HANSCH,C ET AL. (1995)
pKa1.71MERCK INDEX (1996); pK1
Predicted Properties
PropertyValueSource
water solubility2.31e+01 g/lALOGPS
logP-2.6ALOGPS
logP-2.8ChemAxon
logS-0.72ALOGPS
pKa (strongest acidic)2.35ChemAxon
pKa (strongest basic)9.05ChemAxon
physiological charge0ChemAxon
hydrogen acceptor count3ChemAxon
hydrogen donor count3ChemAxon
polar surface area63.32ChemAxon
rotatable bond count2ChemAxon
refractivity28.22ChemAxon
polarizability11.41ChemAxon
number of rings0ChemAxon
bioavailability1ChemAxon
rule of fiveYesChemAxon
Ghose filterNoChemAxon
Veber's ruleNoChemAxon
MDDR-like ruleNoChemAxon
Spectra
SpectraNot Available
References
Synthesis Reference

Alfred Maierhofer, Hans Wagner, “Process for the production of high purity S-carboxymethyl-L-cysteine.” U.S. Patent US4129593, issued May, 1965.

US4129593
General Reference
  1. Bulaj G, Kortemme T, Goldenberg DP: Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry. 1998 Jun 23;37(25):8965-72. Pubmed
  2. Baker DH, Czarnecki-Maulden GL: Pharmacologic role of cysteine in ameliorating or exacerbating mineral toxicities. J Nutr. 1987 Jun;117(6):1003-10. Pubmed
External Links
ResourceLink
KEGG DrugD00026
KEGG CompoundC00097
ChEBI17561
ChEMBLCHEMBL863
PharmGKBPA449173
HETCYS
WikipediaL-Cysteine
ATC CodesR05CB01S01XA08V03AB23
AHFS CodesNot Available
PDB Entries
FDA labelNot Available
MSDSshow(73.2 KB)
Interactions
Drug InteractionsNot Available
Food InteractionsNot Available

Targets

1. Glutamate--cysteine ligase regulatory subunit

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Glutamate--cysteine ligase regulatory subunit P48507 Details

References:

  1. Ashida H, Sawa Y, Shibata H: Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant Cell Physiol. 2005 Apr;46(4):557-62. Epub 2005 Feb 2. Pubmed

2. Glutamate--cysteine ligase catalytic subunit

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Glutamate--cysteine ligase catalytic subunit P48506 Details

References:

  1. Ashida H, Sawa Y, Shibata H: Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant Cell Physiol. 2005 Apr;46(4):557-62. Epub 2005 Feb 2. Pubmed
  2. Srivastava S, Chan C: Application of metabolic flux analysis to identify the mechanisms of free fatty acid toxicity to human hepatoma cell line. Biotechnol Bioeng. 2007 Jul 5;. Pubmed

3. Cysteine dioxygenase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cysteine dioxygenase Q16857 Details

References:

  1. Jin HF, DU SX, Zhao X, Zhang SQ, Tian Y, Bu DF, Tang CS, DU JB: [Significance of endogenous sulfur dioxide in the regulation of cardiovascular system] Beijing Da Xue Xue Bao. 2007 Aug 18;39(4):423-5. Pubmed
  2. Roopnarinesingh ES, Steventon GB, Harris RM, Waring RH, Mitchell SC: Induction of cysteine dioxygenase activity by oral administration of cysteine analogues to the rat: implications for drug efficacy and safety. Drug Metabol Drug Interact. 2005;21(2):75-86. Pubmed
  3. Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z: An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. Pubmed
  4. McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr: Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. Pubmed
  5. Pierce BS, Gardner JD, Bailey LJ, Brunold TC, Fox BG: Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications. Biochemistry. 2007 Jul 24;46(29):8569-78. Epub 2007 Jun 28. Pubmed

4. Aspartate aminotransferase, cytoplasmic

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Aspartate aminotransferase, cytoplasmic P17174 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

5. Cystathionine gamma-lyase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cystathionine gamma-lyase P32929 Details

References:

  1. Fiorucci S, Antonelli E, Mencarelli A, Orlandi S, Renga B, Rizzo G, Distrutti E, Shah V, Morelli A: The third gas: H2S regulates perfusion pressure in both the isolated and perfused normal rat liver and in cirrhosis. Hepatology. 2005 Sep;42(3):539-48. Pubmed
  2. Zhang H, Zhi L, Moore PK, Bhatia M: Role of hydrogen sulfide in cecal ligation and puncture-induced sepsis in the mouse. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1193-201. Epub 2006 Jan 20. Pubmed
  3. Wallace JL, Dicay M, McKnight W, Martin GR: Hydrogen sulfide enhances ulcer healing in rats. FASEB J. 2007 Jul 18;. Pubmed

6. Cystathionine beta-synthase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cystathionine beta-synthase P35520 Details

References:

  1. Zhang H, Zhi L, Moore PK, Bhatia M: Role of hydrogen sulfide in cecal ligation and puncture-induced sepsis in the mouse. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1193-201. Epub 2006 Jan 20. Pubmed
  2. Lowicka E, Beltowski J: Hydrogen sulfide (H2S) – the third gas of interest for pharmacologists. Pharmacol Rep. 2007 Jan-Feb;59(1):4-24. Pubmed
  3. Tamizhselvi R, Moore PK, Bhatia M: Hydrogen sulfide acts as a mediator of inflammation in acute pancreatitis: in vitro studies using isolated mouse pancreatic acinar cells. J Cell Mol Med. 2007 Mar-Apr;11(2):315-26. Pubmed
  4. Oh GS, Pae HO, Lee BS, Kim BN, Kim JM, Kim HR, Jeon SB, Jeon WK, Chae HJ, Chung HT: Hydrogen sulfide inhibits nitric oxide production and nuclear factor-kappaB via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide. Free Radic Biol Med. 2006 Jul 1;41(1):106-19. Epub 2006 Apr 25. Pubmed
  5. Bhatia M, Wong FL, Fu D, Lau HY, Moochhala SM, Moore PK: Role of hydrogen sulfide in acute pancreatitis and associated lung injury. FASEB J. 2005 Apr;19(6):623-5. Epub 2005 Jan 25. Pubmed

7. Cysteine--tRNA ligase, cytoplasmic

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cysteine--tRNA ligase, cytoplasmic P49589 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

8. Methylated-DNA--protein-cysteine methyltransferase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Methylated-DNA--protein-cysteine methyltransferase P16455 Details

References:

  1. Niture SK, Velu CS, Smith QR, Bhat GJ, Srivenugopal KS: Increased expression of the MGMT repair protein mediated by cysteine prodrugs and chemopreventative natural products in human lymphocytes and tumor cell lines. Carcinogenesis. 2007 Feb;28(2):378-89. Epub 2006 Aug 31. Pubmed

9. Glutathione synthetase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Glutathione synthetase P48637 Details

References:

  1. Tanaka T, Halicka HD, Huang X, Traganos F, Darzynkiewicz Z: Constitutive histone H2AX phosphorylation and ATM activation, the reporters of DNA damage by endogenous oxidants. Cell Cycle. 2006 Sep;5(17):1940-5. Epub 2006 Sep 1. Pubmed

10. Thiamine transporter 2

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Thiamine transporter 2 Q9BZV2 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

11. Probable cysteine--tRNA ligase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Probable cysteine--tRNA ligase, mitochondrial Q9HA77 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

12. Cysteine sulfinic acid decarboxylase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cysteine sulfinic acid decarboxylase Q9Y600 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. Chan-Palay V, Lin CT, Palay S, Yamamoto M, Wu JY: Taurine in the mammalian cerebellum: demonstration by autoradiography with [3H]taurine and immunocytochemistry with antibodies against the taurine-synthesizing enzyme, cysteine-sulfinic acid decarboxylase. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2695-9. Pubmed
  4. Guion-Rain M-C, Portemer C, Chatagner F: Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties. Biochim Biophys Acta. 1975 Mar 28;384(1):265-76. Pubmed
  5. Daniels KM, Stipanuk MH: The effect of dietary cysteine level on cysteine metabolism in rats. J Nutr. 1982 Nov;112(11):2130-41. Pubmed

13. Cysteine desulfurase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cysteine desulfurase, mitochondrial Q9Y697 Details

References:

  1. 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
  2. Ding H, Harrison K, Lu J: Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J Biol Chem. 2005 Aug 26;280(34):30432-7. Epub 2005 Jun 28. Pubmed
  3. Ding B, Smith ES, Ding H: Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU. Biochem J. 2005 Aug 1;389(Pt 3):797-802. Pubmed
  4. Yang J, Bitoun JP, Ding H: Interplay of IscA and IscU in biogenesis of iron-sulfur clusters. J Biol Chem. 2006 Sep 22;281(38):27956-63. Epub 2006 Jul 27. Pubmed
  5. Layer G, Ollagnier-de Choudens S, Sanakis Y, Fontecave M: Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J Biol Chem. 2006 Jun 16;281(24):16256-63. Epub 2006 Apr 9. Pubmed

14. Cysteine dioxygenase type 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Cysteine dioxygenase type 1 Q16878 Details

References:

  1. Roopnarinesingh ES, Steventon GB, Harris RM, Waring RH, Mitchell SC: Induction of cysteine dioxygenase activity by oral administration of cysteine analogues to the rat: implications for drug efficacy and safety. Drug Metabol Drug Interact. 2005;21(2):75-86. Pubmed
  2. McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr: Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. Pubmed
  3. Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z: An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. Pubmed
  4. Jin HF, DU SX, Zhao X, Zhang SQ, Tian Y, Bu DF, Tang CS, DU JB: [Significance of endogenous sulfur dioxide in the regulation of cardiovascular system] Beijing Da Xue Xue Bao. 2007 Aug 18;39(4):423-5. Pubmed

Transporters

1. Monocarboxylate transporter 10

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: inhibitor

Components

Name UniProt ID Details
Monocarboxylate transporter 10 Q8TF71 Details

References:

  1. Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. Pubmed

Comments
comments powered by Disqus
Drug created on June 13, 2005 07:24 / Updated on September 24, 2013 13:16