CHEBI:17561 - L-cysteine

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ChEBI Name L-cysteine
ChEBI ID CHEBI:17561
ChEBI ASCII Name L-cysteine
Definition An optically active form of cysteine having L-configuration.
Stars This entity has been manually annotated by the ChEBI Team.
Secondary ChEBI IDs CHEBI:13095, CHEBI:41700, CHEBI:41811, CHEBI:41768, CHEBI:41781, CHEBI:41227, CHEBI:6207, CHEBI:21261
Supplier Information ChemicalBook:CB0330400, eMolecules:533118, Selleckchem:uridine, ZINC000002583633
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Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the formula HOOC−CH(−NH2)−CH2−SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. L‑Cysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστις kýstis, "bladder". The thiol is susceptible to oxidation to give the proteinogenic amino acid derivative formula, which serves an important structural role in many disulfide bondss. In this case, the symbol Cyx is sometimes used. The deprotonated form can generally be described by the symbol Cym as well. When used as a food additive, cysteine has the enzymatic E920. Cysteine is nucleophile by the Greeks UGU and UGC.
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Formula C3H7NO2S
Net Charge 0
Average Mass 121.15800
Monoisotopic Mass 121.01975
InChI InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
InChIKey XUJNEKJLAYXESH-REOHCLBHSA-N
SMILES N[C@@H](CS)C(O)=O
Metabolite of Species Details
Mus musculus (NCBI:txid10090) Source: BioModels - MODEL1507180067 See: PubMed
Saccharomyces cerevisiae (NCBI:txid4932) Source: yeast.sf.net See: PubMed
Escherichia coli (NCBI:txid562) See: PubMed
Homo sapiens (NCBI:txid9606) See: DOI
Roles Classification
Chemical Role(s): Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
Biological Role(s): human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
EC 4.3.1.3 (histidine ammonia-lyase) inhibitor
An EC 4.3.1.* (ammonia-lyase) inhibitor that interferes with the action of histidine ammonia-lyase (EC 4.3.1.3).
flour treatment agent
A food additive which is added to flour or dough to improve baking quality and/or colour.
fundamental metabolite
Any metabolite produced by all living cells.
(via cysteine )
Application(s): flour treatment agent
A food additive which is added to flour or dough to improve baking quality and/or colour.
View more via ChEBI Ontology
ChEBI Ontology
Outgoing L-cysteine (CHEBI:17561) has role EC 4.3.1.3 (histidine ammonia-lyase) inhibitor (CHEBI:77703)
L-cysteine (CHEBI:17561) has role flour treatment agent (CHEBI:64577)
L-cysteine (CHEBI:17561) has role human metabolite (CHEBI:77746)
L-cysteine (CHEBI:17561) is a L-α-amino acid (CHEBI:15705)
L-cysteine (CHEBI:17561) is a cysteine (CHEBI:15356)
L-cysteine (CHEBI:17561) is a proteinogenic amino acid (CHEBI:83813)
L-cysteine (CHEBI:17561) is a serine family amino acid (CHEBI:26650)
L-cysteine (CHEBI:17561) is conjugate acid of L-cysteinate(1−) (CHEBI:32442)
L-cysteine (CHEBI:17561) is conjugate base of L-cysteinium (CHEBI:32445)
L-cysteine (CHEBI:17561) is enantiomer of D-cysteine (CHEBI:16375)
L-cysteine (CHEBI:17561) is tautomer of L-cysteine zwitterion (CHEBI:35235)
Incoming Nα-(L-γ-glutamyl)-hercynyl-L-cysteine sulfoxide (CHEBI:83290) has functional parent L-cysteine (CHEBI:17561)
L-γ-glutamyl-L-cysteine (CHEBI:17515) has functional parent L-cysteine (CHEBI:17561)
L-cysteine derivative (CHEBI:83824) has functional parent L-cysteine (CHEBI:17561)
L-cysteinyl radical (CHEBI:32736) has functional parent L-cysteine (CHEBI:17561)
Ala-Cys (CHEBI:157787) has functional parent L-cysteine (CHEBI:17561)
Ala-Cys-Gly (CHEBI:73345) has functional parent L-cysteine (CHEBI:17561)
Arg-Lys-Cys-Gly (CHEBI:73401) has functional parent L-cysteine (CHEBI:17561)
Arg-Phe-Phe-Cys (CHEBI:73402) has functional parent L-cysteine (CHEBI:17561)
Arg-Thr-Cys-Cys (CHEBI:73404) has functional parent L-cysteine (CHEBI:17561)
Asn-Trp-Cys-His (CHEBI:73415) has functional parent L-cysteine (CHEBI:17561)
Asp-Met-Met-Cys (CHEBI:176848) has functional parent L-cysteine (CHEBI:17561)
benzylpenicilloyl-cysteine (CHEBI:60178) has functional parent L-cysteine (CHEBI:17561)
Cys-Arg (CHEBI:157802) has functional parent L-cysteine (CHEBI:17561)
Cys-Asp-Gly (CHEBI:140231) has functional parent L-cysteine (CHEBI:17561)
Cys-Cys (CHEBI:131608) has functional parent L-cysteine (CHEBI:17561)
Cys-Cys-His-His (CHEBI:73456) has functional parent L-cysteine (CHEBI:17561)
Cys-Gln-Gln (CHEBI:156079) has functional parent L-cysteine (CHEBI:17561)
Cys-Met-Gln (CHEBI:144427) has functional parent L-cysteine (CHEBI:17561)
Cys-Met-Met-Met (CHEBI:73457) has functional parent L-cysteine (CHEBI:17561)
Cys-Met-Phe-His (CHEBI:138508) has functional parent L-cysteine (CHEBI:17561)
Cys-Met-Thr-Tyr (CHEBI:73459) has functional parent L-cysteine (CHEBI:17561)
Cys-Phe-Phe-Gly (CHEBI:73460) has functional parent L-cysteine (CHEBI:17561)
Cys-Pro (CHEBI:73461) has functional parent L-cysteine (CHEBI:17561)
Cys-Ser (CHEBI:73462) has functional parent L-cysteine (CHEBI:17561)
DON-10-S-cysteine (CHEBI:149447) has functional parent L-cysteine (CHEBI:17561)
DON-13-S-cysteine (CHEBI:149448) has functional parent L-cysteine (CHEBI:17561)
Gln-Cys-Cys (CHEBI:144458) has functional parent L-cysteine (CHEBI:17561)
Glu-Cys (CHEBI:156047) has functional parent L-cysteine (CHEBI:17561)
Glu-Cys-Cys (CHEBI:73495) has functional parent L-cysteine (CHEBI:17561)
Leu-Cys (CHEBI:73582) has functional parent L-cysteine (CHEBI:17561)
methyl L-cysteinate (CHEBI:41531) has functional parent L-cysteine (CHEBI:17561)
Phe-Asp-Cys (CHEBI:73629) has functional parent L-cysteine (CHEBI:17561)
Pro-Cys (CHEBI:157881) has functional parent L-cysteine (CHEBI:17561)
Tyr-Cys (CHEBI:157903) has functional parent L-cysteine (CHEBI:17561)
L-cysteinium (CHEBI:32445) is conjugate acid of L-cysteine (CHEBI:17561)
L-cysteinate(1−) (CHEBI:32442) is conjugate base of L-cysteine (CHEBI:17561)
D-cysteine (CHEBI:16375) is enantiomer of L-cysteine (CHEBI:17561)
L-cystein-S-yl group (CHEBI:32793) is substituent group from L-cysteine (CHEBI:17561)
L-cysteine residue (CHEBI:29950) is substituent group from L-cysteine (CHEBI:17561)
L-cysteino group (CHEBI:32448) is substituent group from L-cysteine (CHEBI:17561)
L-cysteinyl group (CHEBI:32447) is substituent group from L-cysteine (CHEBI:17561)
L-cysteine zwitterion (CHEBI:35235) is tautomer of L-cysteine (CHEBI:17561)
IUPAC Name
L-cysteine
Synonyms Sources
(2R)-2-amino-3-mercaptopropanoic acid JCBN
(2R)-2-amino-3-sulfanylpropanoic acid IUPAC
(R)-2-amino-3-mercaptopropanoic acid NIST Chemistry WebBook
C ChEBI
Cys ChEBI
CYSTEINE PDBeChem
E 920 ChEBI
E-920 ChEBI
E920 ChEBI
FREE CYSTEINE PDBeChem
L-2-Amino-3-mercaptopropionic acid KEGG COMPOUND
L-Cystein ChEBI
L-Cysteine KEGG COMPOUND
L-Zystein ChEBI
Manual Xrefs Databases
769 DrugCentral
C00001351 KNApSAcK
C00097 KEGG COMPOUND
CYS PDBeChem
CYS MetaCyc
Cysteine Wikipedia
D00026 KEGG DRUG
DB00151 DrugBank
ECMDB00574 ECMDB
HMDB0000574 HMDB
YMDB00046 YMDB
View more database links
Registry Numbers Types Sources
1721408 Reaxys Registry Number Reaxys
49991 Gmelin Registry Number Gmelin
52-90-4 CAS Registry Number KEGG COMPOUND
52-90-4 CAS Registry Number ChemIDplus
52-90-4 CAS Registry Number NIST Chemistry WebBook
Citations
Bordbar A, Mo ML, Nakayasu ES, Schrimpe-Rutledge AC, Kim YM, Metz TO, Jones MB, Frank BC, Smith RD, Peterson SN, Hyduke DR, Adkins JN, Palsson BO (2012)
Model-driven multi-omic data analysis elucidates metabolic immunomodulators of macrophage activation.
Molecular systems biology 8, 558 [PubMed:22735334]
[show Abstract]
Röther D, Poppe L, Viergutz S, Langer B, Rétey J (2001)
Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida.
European journal of biochemistry 268, 6011-6019 [PubMed:11732994]
[show Abstract]
LEVINE BB (1960)
Studies on the mechanism of the formation of the penicillin antigen. I. Delayed allergic cross-reactions among penicillin G and its degradation products.
The Journal of experimental medicine 112, 1131-1156 [PubMed:13761469]
[show Abstract]
Last Modified
20 April 2021