Identification
- Summary
Cysteine is an amino acid commonly found as a component of total parenteral nutrition and used as an antidote for acetaminophen overdose.
- Brand Names
- Elcys, Freamine 6.9, Freamine III 10, Hepatamine 8, Nephramine, Nouress, Premasol, Primene, Procalamine 3, Trophamine 10 %
- Generic Name
- Cysteine
- DrugBank Accession Number
- DB00151
- Background
A thiol-containing non-essential amino acid that is oxidized to form cystine.
- Type
- Small Molecule
- Groups
- Approved, Nutraceutical
- Structure
Structure for Cysteine (DB00151)
- Weight
- Average: 121.158
Monoisotopic: 121.019749163 - Chemical Formula
- C3H7NO2S
- Synonyms
- (2R)-2-amino-3-mercaptopropanoic acid
- (2R)-2-amino-3-sulfanylpropanoic acid
- (R)-2-Amino-3-mercaptopropanoic acid
- Cisteina
- Cisteinum
- Cys
- Cysteine
- Cysteinum
- Free Cysteine
- L-2-Amino-3-mercaptopropionic acid
- L-Cys
- L-Cystein
- L-cysteine
- L-Zystein
- External IDs
- E 920
- E-920
- E920
- FEMA NO. 3263
- NSC-8746
Pharmacology
- Indication
For the prevention of liver damage and kidney damage associated with overdoses of acetaminophen
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- Contraindications & Blackbox Warnings
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Due 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 action
Cysteine can usually be synthesized by the human body under normal physiological conditions if a sufficient quantity of methionine is available. Cysteine is typically synthesized in the human body when there is sufficient methionine available. Cysteine exhibits antioxidant properties and participates in redox reactions. Cysteine's antioxidant properties are typically expressed in the tripeptide glutathione, which occurs in humans as well as other organisms. Glutathione (GSH) typically requires biosynthesis from its constituent amino acids, cysteine, glycine, and glutamic acid, due to its limited systemic availability. Glutamic acid and glycine are readily available in the diets of most industrialized countries, but the availability of cysteine can be the limiting substrate. In human metabolism, cysteine is also involved in the generation of sulfide present in iron-sulfur clusters and nitrogenase by acting as a precursor. 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).
Target Actions Organism UGlutamate--cysteine ligase regulatory subunit Not Available Humans UGlutamate--cysteine ligase catalytic subunit Not Available Humans UAspartate aminotransferase, cytoplasmic substrateHumans UAspartate aminotransferase, mitochondrial substrateHumans UCystathionine gamma-lyase Not Available Humans UCystathionine beta-synthase Not Available Humans UCysteine--tRNA ligase, cytoplasmic substrateHumans UMethylated-DNA--protein-cysteine methyltransferase Not Available Humans UGlutathione synthetase Not Available Humans UProbable cysteine--tRNA ligase, mitochondrial substrateHumans UCysteine sulfinic acid decarboxylase Not Available Humans UCysteine desulfurase, mitochondrial Not Available Humans UCysteine dioxygenase type 1 Not Available Humans - 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
- Adverse Effects
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Not Available
- Pathways
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- No interactions found.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Product Ingredients
Ingredient UNII CAS InChI Key Cysteine hydrochloride ZT934N0X4W 7048-04-6 QIJRTFXNRTXDIP-JIZZDEOASA-N - International/Other Brands
- Nouress
- Brand Name Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Cysteine Hydrochloride Injection 34.5 mg/1mL Intravenous Baxter Healthcare Corporation 2022-04-29 Not applicable US 
Cysteine Hydrochloride Injection, solution 0.5 g/10mL Intravenous Hospira, Inc. 2006-07-18 2007-10-01 US Elcys Injection, solution 10 mg/1mL Intravenous Exela Pharma Sciences, LLC 2019-05-28 Not applicable US Elcys Injection, solution 50 mg/1mL Intravenous Exela Pharma Sciences, LLC 2023-12-12 Not applicable US L Cysteine HCl Inj 50mg/ml Liquid 50 mg / mL Intravenous Abbott 1984-12-31 1997-08-18 Canada 
- Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image 8.5% Freamine III Cysteine hydrochloride (13.9 mg / 100 mL) + Alanine (600 mg / 100 mL) + Arginine (810 mg / 100 mL) + Glycine (1.19 g / 100 mL) + Histidine (240 mg / 100 mL) + Isoleucine (590 mg / 100 mL) + Leucine (770 mg / 100 mL) + Lysine acetate (620 mg / 100 mL) + Phenylalanine (480 mg / 100 mL) + Proline (950 mg / 100 mL) + Racemethionine (450 mg / 100 mL) + Serine (500 mg / 100 mL) + Threonine (340 mg / 100 mL) + Tryptophan (130 mg / 100 mL) + Valine (560 mg / 100 mL) Liquid Intravenous B. Braun Medical Inc. 1999-05-17 2012-04-16 Canada Aminoderm Poudre Cysteine (2 mg / g) + Glycine (10 mg / g) + Neomycin sulfate (5 mg / g) + Threonine (1 mg / g) Powder Topical Desbergers LtÉe, Division Of Technilab Inc. 1968-12-31 2004-08-09 Canada AMINOSTERIL N-HEPA FOR INTRAVENOUS INFUSION 8% Cysteine (0.52 g/l) + Acetic acid (4.42 g/l) + Alanine (4.64 g/l) + Arginine (10.72 g/l) + Glycine (5.82 g/l) + Histidine (2.8 g/l) + Isoleucine (10.4 g/l) + Leucine (13.09 g/l) + Methionine (1.1 g/l) + Phenylalanine (0.88 g/l) + Proline (5.73 g/l) + Serine (2.24 g/l) + Threonine (4.4 g/l) + Tryptophan (0.7 g/l) + Valine (10.08 g/l) Injection Intravenous FRESENIUS KABI (SINGAPORE) PTE LTD 1998-09-15 Not applicable Singapore 
Aminosyn HF Cysteine hydrochloride (20 mg/100mL) + Alanine (770 mg/100mL) + Arginine (600 mg/100mL) + Glycine (900 mg/100mL) + Histidine (240 mg/100mL) + Isoleucine (900 mg/100mL) + Leucine (1100 mg/100mL) + Lysine acetate (610 mg/100mL) + Methionine (100 mg/100mL) + Phenylalanine (100 mg/100mL) + Proline (800 mg/100mL) + Serine (500 mg/100mL) + Threonine (450 mg/100mL) + Tryptophan (66 mg/100mL) + Valine (840 mg/100mL) Injection, solution Intravenous Hospira, Inc. 2006-01-30 2010-03-01 US Aminoven Infant 10% w/v Cysteine (0.52 g/1000ml) + Alanine (9.3 g/1000ml) + Arginine (7.5 g/1000ml) + Glycine (4.15 g/1000ml) + Histidine (4.76 g/1000ml) + Isoleucine (8 g/1000ml) + Leucine (13 g/1000ml) + Lysine (8.51 g/1000ml) + Malic acid (2.62 g/1000ml) + Methionine (3.12 g/1000ml) + N-acetyltyrosine (5.176 g/1000ml) + Phenylalanine (3.75 g/1000ml) + Proline (9.71 g/1000ml) + Serine (7.67 g/1000ml) + Taurine (0.4 g/1000ml) + Threonine (4.4 g/1000ml) + Tryptophan (2.01 g/1000ml) + Valine (9 g/1000ml) Solution Intravenous FRESENIUS KABI MALAYSIA SDN. BHD 2020-09-08 Not applicable Malaysia 
- Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Distilpure Msm Cysteine (0.02 g/100g) + Biotin (0.02 g/100g) + Cystine (0.05 g/100g) + Methionine (0.02 g/100g) + Thiamine chloride (0.02 g/100g) Powder Topical Mbg Inc (Korea Institute of Science Development) 2017-09-16 2018-09-16 US FREAMINE III %10 1000 ML(SETLI) Cysteine (0.016 %) + Alanine (0.71 %) + Arginine (0.95 %) + Glycine (1.4 %) + Histidine (0.28 %) + Isoleucine (0.69 %) + Leucine (0.91 %) + Lysine (0.73 %) + Methionine (0.53 %) + Phenylalanine (0.56 %) + Proline (1.12 %) + Serine (0.59 %) + Threonine (0.4 %) + Tryptophan (0.15 %) + Valine (0.66 %) Solution Intravenous ECZACIBAŞI-BAXTER HASTANE ÜRÜNLERİ SAN.VE TİC. A.Ş. 2013-01-29 2024-01-23 Turkey 
FREAMINE III %10 1000 ML(SETSIZ) Cysteine (0.016 %) + Alanine (0.71 %) + Arginine (0.95 %) + Glycine (1.4 %) + Histidine (0.28 %) + Isoleucine (0.69 %) + Leucine (0.91 %) + Lysine (0.73 %) + Methionine (0.53 %) + Phenylalanine (0.56 %) + Proline (1.12 %) + Serine (0.59 %) + Threonine (0.4 %) + Tryptophan (0.15 %) + Valine (0.66 %) Solution Intravenous ECZACIBAŞI-BAXTER HASTANE ÜRÜNLERİ SAN.VE TİC. A.Ş. 2013-01-29 2024-01-23 Turkey FREAMINE III %10 500 ML(SETLI) Cysteine (0.016 %) + Alanine (0.71 %) + Arginine (0.95 %) + Glycine (1.4 %) + Histidine (0.28 %) + Isoleucine (0.69 %) + Leucine (0.91 %) + Lysine (0.73 %) + Methionine (0.53 %) + Phenylalanine (0.56 %) + Proline (1.12 %) + Serine (0.59 %) + Threonine (0.4 %) + Tryptophan (0.15 %) + Valine (0.66 %) Solution Intravenous ECZACIBAŞI-BAXTER HASTANE ÜRÜNLERİ SAN.VE TİC. A.Ş. 2013-01-29 2024-01-23 Turkey FREAMINE III %10 500 ML(SETSIZ) Cysteine (0.016 %) + Alanine (0.71 %) + Arginine (0.95 %) + Glycine (1.4 %) + Histidine (0.28 %) + Isoleucine (0.69 %) + Leucine (0.91 %) + Lysine (0.73 %) + Methionine (0.53 %) + Phenylalanine (0.56 %) + Proline (1.12 %) + Serine (0.59 %) + Threonine (0.4 %) + Tryptophan (0.15 %) + Valine (0.66 %) Solution Intravenous ECZACIBAŞI-BAXTER HASTANE ÜRÜNLERİ SAN.VE TİC. A.Ş. 2013-01-29 2024-01-23 Turkey
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as cysteine and derivatives. These are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
- Kingdom
- Organic compounds
- Super Class
- Organic acids and derivatives
- Class
- Carboxylic acids and derivatives
- Sub Class
- Amino acids, peptides, and analogues
- Direct Parent
- Cysteine and derivatives
- Alternative Parents
- L-alpha-amino acids / Amino acids / Monocarboxylic acids and derivatives / Carboxylic acids / Alkylthiols / Organopnictogen compounds / Organic oxides / Monoalkylamines / Hydrocarbon derivatives / Carbonyl compounds
- Substituents
- Aliphatic acyclic compound / Alkylthiol / Alpha-amino acid / Amine / Amino acid / Carbonyl group / Carboxylic acid / Cysteine or derivatives / Hydrocarbon derivative / L-alpha-amino acid
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- proteinogenic amino acid, L-alpha-amino acid, cysteine, serine family amino acid (CHEBI:17561) / Common amino acids (C00097)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- K848JZ4886
- CAS number
- 52-90-4
- InChI Key
- XUJNEKJLAYXESH-REOHCLBHSA-N
- InChI
- InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
- IUPAC Name
- (2R)-2-amino-3-sulfanylpropanoic acid
- SMILES
- N[C@@H](CS)C(O)=O
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 References
- Bulaj G, Kortemme T, Goldenberg DP: Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry. 1998 Jun 23;37(25):8965-72. [Article]
- Baker DH, Czarnecki-Maulden GL: Pharmacologic role of cysteine in ameliorating or exacerbating mineral toxicities. J Nutr. 1987 Jun;117(6):1003-10. [Article]
- External Links
- MSDS
- Download (73.2 KB)
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 4 Active Not Recruiting Prevention Necrotizing Enterocolitis (NEC) / Oral N-acetyl Cysteine / Preterm Neonates and Feeding Intolerance 1 4 Completed Prevention Systemic Inflammatory Response Syndrome (SIRS) 1 4 Completed Treatment Cognitive Deficits / Schizophrenia / Schizophrenia; Negative Type 1 4 Completed Treatment Cystinosis / Kidney Diseases 1 4 Completed Treatment Detection of Different Prognostic Factors and Their Relation With the Outcome / Using New Protocol to Prove the Role of N-acetyl Cysteine and Adequate Supportive Measures in Aluminum Phosphide Poisoning 1
Pharmacoeconomics
- Manufacturers
- Hospira inc
- Packagers
- Amend
- American Regent
- Spectrum Pharmaceuticals
- Dosage Forms
Form Route Strength Injection Intravenous 0.52 g/l Injection, solution Intravenous 0.5 g/10mL Powder Topical Injection, solution Intravenous 10 mg/1mL Solution Intravenous 500.000 mg Injection, solution Intravenous Capsule Oral Injection Intravenous Tablet Oral Liquid Intravenous 50 mg / mL Injection, solution Intravenous 50 mg/1mL Solution Parenteral Injection Intravenous 0.37 g/l Injection Intravenous 34.5 mg/1mL Injection, emulsion Parenteral Injection, emulsion Intravenous Emulsion Intravenous Emulsion Intravenous 0.466 g Solution Oral Injection Intravenous 4 g/l Liquid Intravenous Injection Intravenous 0.21 g/100ml Solution Intravenous Capsule, gelatin coated Oral - Prices
Unit description Cost Unit L-cysteine powder 1.65USD g L-cysteine 50 mg/ml vial 0.4USD ml L-cysteine hcl powder 0.3USD g DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.- Patents
Patent Number Pediatric Extension Approved Expires (estimated) Region US10478453 No 2019-11-19 2039-01-15 US US10493051 No 2019-12-03 2039-03-15 US US10543186 No 2020-01-28 2039-03-15 US US10583155 No 2020-03-10 2039-01-15 US US10653719 No 2020-05-19 2039-01-15 US US10702490 No 2020-07-07 2039-03-15 US US10905714 No 2021-02-02 2039-01-15 US US10905713 No 2021-02-02 2039-01-15 US US10912795 No 2021-02-09 2039-01-15 US US10918662 No 2021-02-16 2039-01-15 US US10933089 No 2021-03-02 2039-01-15 US US11045438 No 2021-06-29 2039-03-15 US US11510942 No 2019-01-15 2039-01-15 US US11510941 No 2019-01-15 2039-01-15 US US11648262 No 2019-01-15 2039-01-15 US US11642370 No 2019-01-15 2039-01-15 US US11684636 No 2019-01-15 2039-01-15 US US11679125 No 2019-01-15 2039-01-15 US US11826383 No 2019-01-15 2039-01-15 US
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 240 dec °C PhysProp water solubility 2.77E+005 mg/L (at 25 °C) BEILSTEIN logP -2.49 HANSCH,C ET AL. (1995) pKa 1.71 MERCK INDEX (1996); pK1 - Predicted Properties
Property Value Source Water Solubility 23.1 mg/mL ALOGPS logP -2.6 ALOGPS logP -2.8 Chemaxon logS -0.72 ALOGPS pKa (Strongest Acidic) 2.35 Chemaxon pKa (Strongest Basic) 9.05 Chemaxon Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 3 Chemaxon Hydrogen Donor Count 3 Chemaxon Polar Surface Area 63.32 Å2 Chemaxon Rotatable Bond Count 2 Chemaxon Refractivity 28.22 m3·mol-1 Chemaxon Polarizability 11.41 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - 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 inhibitor Non-inhibitor 0.9584 CYP450 2D6 inhibitor Non-inhibitor 0.9665 CYP450 2C19 inhibitor Non-inhibitor 0.9634 CYP450 3A4 inhibitor 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
Spectra
- Mass Spec (NIST)
- Download (8.4 KB)
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 116.6005377 predictedDarkChem Lite v0.1.0 [M-H]- 116.5967377 predictedDarkChem Lite v0.1.0 [M-H]- 116.7254377 predictedDarkChem Lite v0.1.0 [M-H]- 120.07873 predictedDeepCCS 1.0 (2019) [M-H]- 116.6005377 predictedDarkChem Lite v0.1.0 [M-H]- 116.5967377 predictedDarkChem Lite v0.1.0 [M-H]- 116.7254377 predictedDarkChem Lite v0.1.0 [M-H]- 120.07873 predictedDeepCCS 1.0 (2019) [M+H]+ 117.8203377 predictedDarkChem Lite v0.1.0 [M+H]+ 117.8588377 predictedDarkChem Lite v0.1.0 [M+H]+ 117.8339377 predictedDarkChem Lite v0.1.0 [M+H]+ 123.015854 predictedDeepCCS 1.0 (2019) [M+H]+ 117.8203377 predictedDarkChem Lite v0.1.0 [M+H]+ 117.8588377 predictedDarkChem Lite v0.1.0 [M+H]+ 117.8339377 predictedDarkChem Lite v0.1.0 [M+H]+ 123.015854 predictedDeepCCS 1.0 (2019) [M+Na]+ 116.8763377 predictedDarkChem Lite v0.1.0 [M+Na]+ 132.8321438 predictedDarkChem Standard v0.1.0 [M+Na]+ 116.8474377 predictedDarkChem Lite v0.1.0 [M+Na]+ 131.58159 predictedDeepCCS 1.0 (2019) [M+Na]+ 116.8763377 predictedDarkChem Lite v0.1.0 [M+Na]+ 132.8321438 predictedDarkChem Standard v0.1.0 [M+Na]+ 116.8474377 predictedDarkChem Lite v0.1.0 [M+Na]+ 131.58159 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Glutamate-cysteine ligase catalytic subunit binding
- Specific Function
- Not Available
- Gene Name
- GCLM
- Uniprot ID
- P48507
- Uniprot Name
- Glutamate--cysteine ligase regulatory subunit
- Molecular Weight
- 30726.745 Da
References
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Magnesium ion binding
- Specific Function
- Not Available
- Gene Name
- GCLC
- Uniprot ID
- P48506
- Uniprot Name
- Glutamate--cysteine ligase catalytic subunit
- Molecular Weight
- 72765.14 Da
References
- 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. [Article]
- 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. 2008 Feb 1;99(2):399-410. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- 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
- Wen YD, Wang H, Zhu YZ: The Drug Developments of Hydrogen Sulfide on Cardiovascular Disease. Oxid Med Cell Longev. 2018 Jul 29;2018:4010395. doi: 10.1155/2018/4010395. eCollection 2018. [Article]
- Cooper AJ, Bruschi SA, Iriarte A, Martinez-Carrion M: Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions. Biochem J. 2002 Nov 15;368(Pt 1):253-61. doi: 10.1042/BJ20020531. [Article]
- Gaskin PJ, Adcock HJ, Buckberry LD, Teesdale-Spittle PH, Shaw PN: The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes. Hum Exp Toxicol. 1995 May;14(5):422-7. doi: 10.1177/096032719501400506. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- 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
- Gaskin PJ, Adcock HJ, Buckberry LD, Teesdale-Spittle PH, Shaw PN: The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes. Hum Exp Toxicol. 1995 May;14(5):422-7. doi: 10.1177/096032719501400506. [Article]
- Cooper AJ, Bruschi SA, Iriarte A, Martinez-Carrion M: Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions. Biochem J. 2002 Nov 15;368(Pt 1):253-61. doi: 10.1042/BJ20020531. [Article]
- Wen YD, Wang H, Zhu YZ: The Drug Developments of Hydrogen Sulfide on Cardiovascular Disease. Oxid Med Cell Longev. 2018 Jul 29;2018:4010395. doi: 10.1155/2018/4010395. eCollection 2018. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- 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
- 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. [Article]
- 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. [Article]
- Wallace JL, Dicay M, McKnight W, Martin GR: Hydrogen sulfide enhances ulcer healing in rats. FASEB J. 2007 Dec;21(14):4070-6. Epub 2007 Jul 18. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- 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
- 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. [Article]
- Lowicka E, Beltowski J: Hydrogen sulfide (H2S) - the third gas of interest for pharmacologists. Pharmacol Rep. 2007 Jan-Feb;59(1):4-24. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Trna binding
- Specific Function
- Not Available
- Gene Name
- CARS
- Uniprot ID
- P49589
- Uniprot Name
- Cysteine--tRNA ligase, cytoplasmic
- Molecular Weight
- 85472.665 Da
References
- Kuo ME, Theil AF, Kievit A, Malicdan MC, Introne WJ, Christian T, Verheijen FW, Smith DEC, Mendes MI, Hussaarts-Odijk L, van der Meijden E, van Slegtenhorst M, Wilke M, Vermeulen W, Raams A, Groden C, Shimada S, Meyer-Schuman R, Hou YM, Gahl WA, Antonellis A, Salomons GS, Mancini GMS: Cysteinyl-tRNA Synthetase Mutations Cause a Multi-System, Recessive Disease That Includes Microcephaly, Developmental Delay, and Brittle Hair and Nails. Am J Hum Genet. 2019 Mar 7;104(3):520-529. doi: 10.1016/j.ajhg.2019.01.006. Epub 2019 Feb 26. [Article]
- Davidson E, Caffarella J, Vitseva O, Hou YM, King MP: Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase. Biol Chem. 2001 Mar;382(3):399-406. [Article]
- Akaike T, Ida T, Wei FY, Nishida M, Kumagai Y, Alam MM, Ihara H, Sawa T, Matsunaga T, Kasamatsu S, Nishimura A, Morita M, Tomizawa K, Nishimura A, Watanabe S, Inaba K, Shima H, Tanuma N, Jung M, Fujii S, Watanabe Y, Ohmuraya M, Nagy P, Feelisch M, Fukuto JM, Motohashi H: Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Nat Commun. 2017 Oct 27;8(1):1177. doi: 10.1038/s41467-017-01311-y. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Methyltransferase activity
- Specific Function
- Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 p...
- Gene Name
- MGMT
- Uniprot ID
- P16455
- Uniprot Name
- Methylated-DNA--protein-cysteine methyltransferase
- Molecular Weight
- 21645.83 Da
References
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein homodimerization activity
- Specific Function
- Not Available
- Gene Name
- GSS
- Uniprot ID
- P48637
- Uniprot Name
- Glutathione synthetase
- Molecular Weight
- 52384.325 Da
References
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Metal ion binding
- Specific Function
- Not Available
- Gene Name
- CARS2
- Uniprot ID
- Q9HA77
- Uniprot Name
- Probable cysteine--tRNA ligase, mitochondrial
- Molecular Weight
- 62223.345 Da
References
- Akaike T, Ida T, Wei FY, Nishida M, Kumagai Y, Alam MM, Ihara H, Sawa T, Matsunaga T, Kasamatsu S, Nishimura A, Morita M, Tomizawa K, Nishimura A, Watanabe S, Inaba K, Shima H, Tanuma N, Jung M, Fujii S, Watanabe Y, Ohmuraya M, Nagy P, Feelisch M, Fukuto JM, Motohashi H: Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Nat Commun. 2017 Oct 27;8(1):1177. doi: 10.1038/s41467-017-01311-y. [Article]
- Kuo ME, Theil AF, Kievit A, Malicdan MC, Introne WJ, Christian T, Verheijen FW, Smith DEC, Mendes MI, Hussaarts-Odijk L, van der Meijden E, van Slegtenhorst M, Wilke M, Vermeulen W, Raams A, Groden C, Shimada S, Meyer-Schuman R, Hou YM, Gahl WA, Antonellis A, Salomons GS, Mancini GMS: Cysteinyl-tRNA Synthetase Mutations Cause a Multi-System, Recessive Disease That Includes Microcephaly, Developmental Delay, and Brittle Hair and Nails. Am J Hum Genet. 2019 Mar 7;104(3):520-529. doi: 10.1016/j.ajhg.2019.01.006. Epub 2019 Feb 26. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Daniels KM, Stipanuk MH: The effect of dietary cysteine level on cysteine metabolism in rats. J Nutr. 1982 Nov;112(11):2130-41. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- 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
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Ferrous iron binding
- Specific Function
- Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations...
- Gene Name
- CDO1
- Uniprot ID
- Q16878
- Uniprot Name
- Cysteine dioxygenase type 1
- Molecular Weight
- 22971.745 Da
References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Transporters
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Transporter activity
- Specific Function
- Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells (By similarity).
- Gene Name
- SLC16A10
- Uniprot ID
- Q8TF71
- Uniprot Name
- Monocarboxylate transporter 10
- Molecular Weight
- 55492.07 Da
References
- 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. [Article]
Drug created at June 13, 2005 13:24 / Updated at February 20, 2024 23:55