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Human Metabolome Database Version 3.5

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Showing metabocard for L-Cysteine (HMDB00574)

Record Information
Version 3.5
Creation Date 2005-11-16 08:48:42 -0700
Update Date 2013-05-13 17:03:59 -0600
HMDB ID HMDB00574
Secondary Accession Numbers None
Metabolite Identification
Common Name L-Cysteine
Description Cysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible: as reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. N-acetyl-L-cysteine (NAC) is a form of cysteine where an acetyl group is attached to cysteine's nitrogen atom and is sold as a dietary supplement. Cysteine is named after cystine, which comes from the Greek word kustis meaning bladder - cystine was first isolated from kidney stones. As cysteine contains a sulphydryl group, it can undergo redox reactions. Oxidation of cysteine can produce a disulfide bond with another thiol, or further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead and cadmium tightly. 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. (http://en.wikipedia.org/wiki/Cysteine). Cysteine is important in energy metabolism. As cystine, it is a structural component of many tissues and hormones. Cysteine has clinical uses ranging from baldness to psoriasis to preventing smoker's hack. In some cases, oral cysteine therapy has proved excellent for treatment of asthmatics, enabling them to stop theophylline and other medications. Cysteine also enhances the effect of topically applied silver, tin and zinc salts in preventing dental cavities. In the future, cysteine may play a role in the treatment of cobalt toxicity, diabetes, psychosis, cancer and seizures. (http://www.dcnutrition.com/AminoAcids/).
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
  1. (+)-2-Amino-3-mercaptopropionic acid
  2. (2R)-2-amino-3-mercaptopropanoate
  3. (2R)-2-amino-3-mercaptopropanoic acid
  4. (2R)-2-amino-3-sulfanylpropanoate
  5. (2R)-2-amino-3-sulfanylpropanoic acid
  6. (R)-(+)-cysteine
  7. (R)-2-amino-3-mercapto-Propanoate
  8. (R)-2-amino-3-mercapto-Propanoic acid
  9. (R)-2-Amino-3-mercaptopropanoate
  10. (R)-2-Amino-3-mercaptopropanoic acid
  11. (R)-cysteine
  12. 2-Amino-3-mercaptopropanoate
  13. 2-Amino-3-mercaptopropanoic acid
  14. 2-Amino-3-mercaptopropionate
  15. 2-Amino-3-mercaptopropionic acid
  16. 3-Mercapto-L-Alanine
  17. Acetylcysteine
  18. alpha-Amino-beta-thiolpropionic acid
  19. B-Mercaptoalanine
  20. beta-Mercaptoalanine
  21. Carbocysteine
  22. Cisteina
  23. Cisteinum
  24. Cystein
  25. Cysteine
  26. Cysteinum
  27. Free cysteine
  28. Half-cystine
  29. L Cysteine
  30. L-(+)-Cysteine
  31. L-2-Amino-3-mercaptopropanoate
  32. L-2-Amino-3-mercaptopropanoic acid
  33. L-2-Amino-3-mercaptopropionic acid
  34. L-Cystein
  35. L-Cysteine
  36. Polycysteine
  37. Thioserine
Chemical Formula C3H7NO2S
Average Molecular Weight 121.158
Monoisotopic Molecular Weight 121.019749163
IUPAC Name (2R)-2-amino-3-sulfanylpropanoic acid
Traditional IUPAC Name L-cysteine
CAS Registry Number 52-90-4
SMILES N[C@@H](CS)C(O)=O
InChI Identifier InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
InChI Key XUJNEKJLAYXESH-REOHCLBHSA-N
Chemical Taxonomy
Kingdom Organic Compounds
Super Class Amino Acids, Peptides, and Analogues
Class Amino Acids and Derivatives
Sub Class Alpha Amino Acids and Derivatives
Other Descriptors
  • Aliphatic Acyclic Compounds
  • Common amino acids(KEGG)
  • cysteine zwitterion(ChEBI)
Substituents
  • Alkylthiol
  • Carboxylic Acid
  • Primary Aliphatic Amine (Alkylamine)
  • Thiol (Sulfanyl Compound)
Direct Parent Alpha Amino Acids and Derivatives
Ontology
Status Detected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Cysteine metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Methionine metabolism
  • Component of Nitrogen metabolism
  • Component of Selenoamino acid metabolism
  • Component of Taurine and hypotaurine metabolism
Application Not Available
Cellular locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
Physical Properties
State Solid
Experimental Properties
Property Value Reference
Melting Point 220 °C Not Available
Boiling Point Not Available Not Available
Water Solubility 277 mg/mL at 25 °C BEILSTEIN
LogP -2.49 HANSCH,C ET AL. (1995)
Predicted Properties
Property Value Source
Water Solubility 23.1 g/L ALOGPS
LogP -2.57 ALOGPS
LogP -2.8 ChemAxon
LogS -0.72 ALOGPS
pKa (strongest acidic) 2.35 ChemAxon
pKa (strongest basic) 9.05 ChemAxon
Hydrogen Acceptor Count 3 ChemAxon
Hydrogen Donor Count 3 ChemAxon
Polar Surface Area 63.32 A2 ChemAxon
Rotatable Bond Count 2 ChemAxon
Refractivity 28.22 ChemAxon
Polarizability 11.46 ChemAxon
Formal Charge 0 ChemAxon
Physiological Charge 0 ChemAxon
Spectra
Gas-MS Spectrum
13C NMR Spectrum
1H NMR Spectrum
MS/MS Spectrum Quattro_QQQ 10
MS/MS Spectrum Quattro_QQQ 25
MS/MS Spectrum Quattro_QQQ 40
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic)
MS/MS Spectrum GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)
MS/MS Spectrum GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)
MS/MS Spectrum GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)
MS/MS Spectrum GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies )
[1H,1H] 2D NMR Spectrum
[1H,13C] 2D NMR Spectrum
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Urine
Tissue Location
  • Muscle
  • Skeletal Muscle
  • Fibroblasts
  • Intestine
  • Neuron
  • Placenta
  • Testes
  • Kidney
  • Epidermis
  • Thyroid Gland
  • Myelin
  • Prostate
  • Adrenal Cortex
  • Platelet
  • Spleen
Pathways
Name SMPDB Link KEGG Link
Glutathione Metabolism SMP00015 map00480 Link_out
Glycine and Serine Metabolism SMP00004 map00260 Link_out
Methionine Metabolism SMP00033 map00270 Link_out
Taurine and Hypotaurine Metabolism SMP00021 map00430 Link_out
Cysteine Metabolism SMP00013 map00270 Link_out
Pantothenate and CoA Biosynthesis SMP00027 map00770 Link_out
Transcription/Translation SMP00019 Not Available
Normal Concentrations
Biofluid Status Value Age Sex Condition Comments
Blood Detected and Quantified
Article_icon
197.00 +/- 56.00 uM Adolescent (13-18 years old) Both Normal Not Available
Blood Detected and Quantified
Article_icon
131.00 +/- 40.00 uM Infant (0-1 year old) Both Normal Not Available
Blood Detected and Quantified
Article_icon
210.00 +/- 40.00 uM Children (1-13 year old) Both Normal Not Available
Blood Detected and Quantified
Article_icon
212.00 +/- 23.00 uM Adult (>18 years old) Both Normal Not Available
Blood Detected and Quantified
Article_icon
52.0 (41.0-63.0) uM Adult (>18 years old) Both Normal Not Available
Blood Detected and Quantified
Article_icon
33.5 +/- 10.3 uM Adult (>18 years old) Not Specified Normal Not Available
Cerebrospinal Fluid (CSF) Detected and Quantified
Article_icon
0.054 (0.017-0.108) uM Adult (>18 years old) Not Specified Normal Not Available
Urine Detected and Quantified
3.322 (1.447-5.197) umol/mmol creatinine Adult (>18 years old) Both Normal Not Available
Urine Detected and Quantified
Article_icon
30.32 +/- 24.58 umol/mmol creatinine Infant (0-1 year old) Both Normal Not Available
Urine Detected and Quantified
Article_icon
81.0 (36.7-147.6) umol/mmol creatinine Adult (>18 years old) Both Normal by HPLC-FLD
Urine Detected and Quantified
Article_icon
32.00 +/- 10.00 umol/mmol creatinine Infant (0-1 year old) Both Normal Not Available
Urine Detected and Quantified
Article_icon
28.00 +/- 9.00 umol/mmol creatinine Children (1-13 year old) Both Normal Not Available
Urine Detected and Quantified
Article_icon
34.4 +/- 11.00 umol/mmol creatinine Adolescent (13-18 years old) Both Normal Not Available
Urine Detected and Quantified
Article_icon
33.4 +/- 15.5 umol/mmol creatinine Adult (>18 years old) Both Normal Not Available
Urine Detected and Quantified
Article_icon
65.8 (23.1-134.5) umol/mmol creatinine Adult (>18 years old) Both Normal urine by NMR
Urine Detected and Quantified
Article_icon
14.9 umol/mmol creatinine Adult (>18 years old) Both Normal Not Available
Abnormal Concentrations
Biofluid Status Value Age Sex Condition Comments
Blood Detected and Quantified
Article_icon
0.355 (0.157-1.146) uM Adult (>18 years old) Not Specified Multiple sclerosis Not Available
Blood Detected and Quantified
Article_icon
0.420 (0.154-0.874) uM Adult (>18 years old) Not Specified Stroke Not Available
Blood Detected and Quantified
Article_icon
0.415 (0.199-1.038) uM Adult (>18 years old) Not Specified Peripheral neuropathy Not Available
Blood Detected and Quantified
Article_icon
0.491 (0.247-1.764) uM Adult (>18 years old) Not Specified Dementia (Alzheimer's and non-Alzheimer's) Not Available
Blood Detected and Quantified
Article_icon
13.0 (10.0-16.0) uM Adult (>18 years old) Both AIDS Not Available
Blood Detected and Quantified
Article_icon
12.81 +/- 2.17 uM Elderly (>65 years old) Both Alzheimer's Disease Not Available
Cerebrospinal Fluid (CSF) Detected and Quantified
Article_icon
0.042 (0.022-0.10) uM Adult (>18 years old) Not Specified Multiple sclerosis Not Available
Cerebrospinal Fluid (CSF) Detected and Quantified
Article_icon
0.048 (0.018-0.10) uM Adult (>18 years old) Not Specified Stroke Not Available
Cerebrospinal Fluid (CSF) Detected and Quantified
Article_icon
0.034 (0.018-0.075) uM Adult (>18 years old) Not Specified Peripheral neuropathy Not Available
Cerebrospinal Fluid (CSF) Detected and Quantified
Article_icon
0.047 (0.025-0.125) uM Adult (>18 years old) Not Specified Dementia (Alzheimer's and non-Alzheimer's) Not Available
Associated Disorders and Diseases
Disease References
AIDS
  • Naisbitt DJ, Vilar FJ, Stalford AC, Wilkins EG, Pirmohamed M, Park BK: Plasma cysteine deficiency and decreased reduction of nitrososulfamethoxazole with HIV infection. AIDS Res Hum Retroviruses. 2000 Dec 10;16(18):1929-38. Pubmed: 11153075 Link_out
    Multiple sclerosis
    • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. Pubmed: 17384003 Link_out
      Stroke
      • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. Pubmed: 17384003 Link_out
        Peripheral neuropathy
        • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. Pubmed: 17384003 Link_out
          Dementia
          • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. Pubmed: 17384003 Link_out
            Associated OMIM IDs
            DrugBank ID DB00151 Link_out
            Phenol Explorer Compound ID Not Available
            Phenol Explorer Metabolite ID Not Available
            FoodDB ID FDB012678
            KNApSAcK ID C00001351 Link_out
            Chemspider ID 5653 Link_out
            KEGG Compound ID C00097 Link_out
            BioCyc ID CYS Link_out
            BiGG ID 33843 Link_out
            Wikipedia Link L-Cysteine Link_out
            NuGOwiki Link HMDB00574 Link_out
            Metagene Link HMDB00574 Link_out
            METLIN ID 5556 Link_out
            PubChem Compound 5862 Link_out
            PDB ID CYS Link_out
            ChEBI ID 17561 Link_out
            References
            Synthesis Reference Kumagai, Hidehiko; Tanaka, Hideyuki; Sejima, Shunsuke; Yamada, Hideaki. Elimination and replacement reactions of b-chloro-L-alanine by cysteine desulfhydrase from Aerobacter aerogenes. Agricultural and Biological Chemistry (1977), 41(10), 2071-5.
            Material Safety Data Sheet (MSDS) Download (PDF)
            General References
            1. Sandmann J, Schwedhelm KS, Tsikas D: Specific transport of S-nitrosocysteine in human red blood cells: Implications for formation of S-nitrosothiols and transport of NO bioactivity within the vasculature. FEBS Lett. 2005 Aug 1;579(19):4119-24. Pubmed: 16023102 Link_out
            2. Paivalainen S, Suokas M, Lahti O, Heape AM: Degraded myelin-associated glycoprotein (dMAG) formation from pure human brain myelin-associated glycoprotein (MAG) is not mediated by calpain or cathepsin L-like activities. J Neurochem. 2003 Feb;84(3):533-45. Pubmed: 12558973 Link_out
            3. Iyer S, Leonidas DD, Swaminathan GJ, Maglione D, Battisti M, Tucci M, Persico MG, Acharya KR: The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution. J Biol Chem. 2001 Apr 13;276(15):12153-61. Epub 2000 Nov 7. Pubmed: 11069911 Link_out
            4. Nishiya Y, Yoshida Y, Yoshimura M, Fukamachi H, Nakano Y: Homogeneous enzymatic assay for L-cysteine with betaC-S lyase. Biosci Biotechnol Biochem. 2005 Nov;69(11):2244-6. Pubmed: 16306712 Link_out
            5. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. Pubmed: 12297216 Link_out
            6. Santamaria I, Velasco G, Cazorla M, Fueyo A, Campo E, Lopez-Otin C: Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 1998 Apr 15;58(8):1624-30. Pubmed: 9563472 Link_out
            7. Eriksson A, Tohonen V, Wedell A, Nordqvist K: Isolation of the human testatin gene and analysis in patients with abnormal gonadal development. Mol Hum Reprod. 2002 Jan;8(1):8-15. Pubmed: 11756564 Link_out
            8. Kaminska J, Wisniewska A, Koscielak J: Chemical modifications of alpha1,6-fucosyltransferase define amino acid residues of catalytic importance. Biochimie. 2003 Mar-Apr;85(3-4):303-10. Pubmed: 12770769 Link_out
            9. Li Y, Gamper N, Shapiro MS: Single-channel analysis of KCNQ K+ channels reveals the mechanism of augmentation by a cysteine-modifying reagent. J Neurosci. 2004 Jun 2;24(22):5079-90. Pubmed: 15175377 Link_out
            10. Lindzen M, Gottschalk KE, Fuzesi M, Garty H, Karlish SJ: Structural interactions between FXYD proteins and Na+,K+-ATPase: alpha/beta/FXYD subunit stoichiometry and cross-linking. J Biol Chem. 2006 Mar 3;281(9):5947-55. Epub 2005 Dec 21. Pubmed: 16373350 Link_out
            11. Norris FA, Wilson MP, Wallis TS, Galyov EE, Majerus PW: SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase. Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14057-9. Pubmed: 9826652 Link_out
            12. Kersemans V, Cornelissen B, Kersemans K, Bauwens M, Achten E, Dierckx RA, Mertens J, Slegers G: In vivo characterization of 123/125I-2-iodo-L-phenylalanine in an R1M rhabdomyosarcoma athymic mouse model as a potential tumor tracer for SPECT. J Nucl Med. 2005 Mar;46(3):532-9. Pubmed: 15750170 Link_out
            13. Foss CA, Mease RC, Fan H, Wang Y, Ravert HT, Dannals RF, Olszewski RT, Heston WD, Kozikowski AP, Pomper MG: Radiolabeled small-molecule ligands for prostate-specific membrane antigen: in vivo imaging in experimental models of prostate cancer. Clin Cancer Res. 2005 Jun 1;11(11):4022-8. Pubmed: 15930336 Link_out
            14. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. Pubmed: 6696735 Link_out
            15. Kozaki K, Miyaishi O, Asai N, Iida K, Sakata K, Hayashi M, Nishida T, Matsuyama M, Shimizu S, Kaneda T, et al.: Tissue distribution of ERp61 and association of its increased expression with IgG production in hybridoma cells. Exp Cell Res. 1994 Aug;213(2):348-58. Pubmed: 8050492 Link_out
            16. Amberger VR, Hensel T, Ogata N, Schwab ME: Spreading and migration of human glioma and rat C6 cells on central nervous system myelin in vitro is correlated with tumor malignancy and involves a metalloproteolytic activity. Cancer Res. 1998 Jan 1;58(1):149-58. Pubmed: 9426071 Link_out
            17. Zhang JT, Li QX, Wang D, Zhu ZL, Yang YH, Cui DS, Wang MW, Sun XF: Up-regulation of PINCH in the stroma of oral squamous cell carcinoma predicts nodal metastasis. Oncol Rep. 2005 Dec;14(6):1519-22. Pubmed: 16273248 Link_out
            18. Taveau M, Bourg N, Sillon G, Roudaut C, Bartoli M, Richard I: Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol Cell Biol. 2003 Dec;23(24):9127-35. Pubmed: 14645524 Link_out
            19. Yu FH, Westenbroek RE, Silos-Santiago I, McCormick KA, Lawson D, Ge P, Ferriera H, Lilly J, DiStefano PS, Catterall WA, Scheuer T, Curtis R: Sodium channel beta4, a new disulfide-linked auxiliary subunit with similarity to beta2. J Neurosci. 2003 Aug 20;23(20):7577-85. Pubmed: 12930796 Link_out
            20. Naisbitt DJ, Vilar FJ, Stalford AC, Wilkins EG, Pirmohamed M, Park BK: Plasma cysteine deficiency and decreased reduction of nitrososulfamethoxazole with HIV infection. AIDS Res Hum Retroviruses. 2000 Dec 10;16(18):1929-38. Pubmed: 11153075 Link_out
            21. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411 Link_out
            Enzymes
            Name: Aspartate aminotransferase, cytoplasmic
            Reactions:
            • L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
            Gene Name: GOT1
            Uniprot ID: P17174 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Aspartate aminotransferase, mitochondrial
            Reactions:
            • L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
            Gene Name: GOT2
            Uniprot ID: P00505 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Aminopeptidase N
            Reactions:
            • Release of an N-terminal amino acid, Xaa!Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide ALL_REAC (other) R00899 R04951 COFACTOR Manganese [CPD:C00034]
            • Zinc [CPD:C00038]
            Gene Name: ANPEP
            Uniprot ID: P15144 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Glutamate--cysteine ligase catalytic subunit
            Reactions:
            • ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine [RN:R00894]
            Gene Name: GCLC
            Uniprot ID: P48506 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Glutamate--cysteine ligase regulatory subunit
            Reactions:
            • --- []
            Gene Name: GCLM
            Uniprot ID: P48507 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Cystathionine gamma-lyase
            Reactions:
            • (1) L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate (overall reaction) [RN:R01001]
            • (2) (1a) L-cystathionine = L-cysteine + 2-ammoniobut-2-enoate [RN:R08632]
            • (3) (1b) 2-ammoniobut-2-enoate + H2O = 2-oxobutanoate + NH3 (spontaneous) [RN:R08637]
            Gene Name: CTH
            Uniprot ID: P32929 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Glutaminyl-peptide cyclotransferase
            Reactions:
            • L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3 [RN:R04058]
            Gene Name: QPCT
            Uniprot ID: Q16769 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Cystathionine beta-synthase
            Reactions:
            • L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
            Gene Name: CBS
            Uniprot ID: P35520 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Glutathione synthetase
            Reactions:
            • ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione [RN:R00497]
            Gene Name: GSS
            Uniprot ID: P48637 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Cytosol aminopeptidase
            Reactions:
            • Release of N-terminal proline from a peptide ALL_REAC (other) R00135 COFACTOR Manganese [CPD:C00034]
            Gene Name: LAP3
            Uniprot ID: P28838 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Cysteine sulfinic acid decarboxylase
            Reactions:
            • 3-sulfino-L-alanine = hypotaurine + CO2 [RN:R02466]
            Gene Name: CSAD
            Uniprot ID: Q9Y600 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Cysteine dioxygenase type 1
            Reactions:
            • L-cysteine + O2 = 3-sulfinoalanine [RN:R00893]
            Gene Name: CDO1
            Uniprot ID: Q16878 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Methylated-DNA--protein-cysteine methyltransferase
            Reactions:
            • DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine [RN:R04314]
            Gene Name: MGMT
            Uniprot ID: P16455 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Cysteine desulfurase, mitochondrial
            Reactions:
            • L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine [RN:R07460]
            Gene Name: NFS1
            Uniprot ID: Q9Y697 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: Phosphopantothenoylcysteine synthetase
            Reactions:
            • --- - CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine [RN:R04231]
            Gene Name: PPCS
            Uniprot ID: Q9HAB8 Link_out
            Protein Sequence: FASTA
            Gene Sequence: FASTA
            Name: 4F2 cell-surface antigen heavy chain
            Reactions:
              Gene Name: SLC3A2
              Uniprot ID: P08195 Link_out
              Protein Sequence: FASTA
              Gene Sequence: FASTA
              Name: Thiamine transporter 2
              Reactions:
                Gene Name: SLC19A3
                Uniprot ID: Q9BZV2 Link_out
                Protein Sequence: FASTA
                Gene Sequence: FASTA
                Name: Probable cysteinyl-tRNA synthetase, mitochondrial
                Reactions:
                • ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys [RN:R03650]
                Gene Name: CARS2
                Uniprot ID: Q9HA77 Link_out
                Protein Sequence: FASTA
                Gene Sequence: FASTA
                Name: Prenylcysteine oxidase 1
                Reactions:
                • an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2 [RN:R07360]
                Gene Name: PCYOX1
                Uniprot ID: Q9UHG3 Link_out
                Protein Sequence: FASTA
                Gene Sequence: FASTA
                Name: Cysteinyl-tRNA synthetase, isoform CRA_e
                Reactions:
                • --- - ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys [RN:R03650]
                Gene Name: DKFZp686F1612
                Uniprot ID: P49589 Link_out
                Protein Sequence: FASTA
                Gene Sequence: FASTA
                Name: Gamma-glutamylcyclotransferase
                Reactions:
                • (gamma-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid [RN:R03749]
                Gene Name: GGCT
                Uniprot ID: O75223 Link_out
                Protein Sequence: FASTA
                Gene Sequence: FASTA
                Name: Cysteine dioxygenase
                Reactions:
                • L-cysteine + O2 = 3-sulfinoalanine [RN:R00893]
                Gene Name: CDO-1
                Uniprot ID: Q16857 Link_out
                Protein Sequence: FASTA
                Transporters
                Name: Large neutral amino acids transporter small subunit 2
                Reactions:
                • --- []
                Gene Name: SLC7A8
                Uniprot ID: Q9UHI5 Link_out
                Protein Sequence: FASTA
                Gene Sequence: FASTA
                Name: Monocarboxylate transporter 10
                Reactions:
                  Gene Name: SLC16A10
                  Uniprot ID: Q8TF71 Link_out
                  Protein Sequence: FASTA
                  Gene Sequence: FASTA