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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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Read full article at Wikipedia
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InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 |
XUJNEKJLAYXESH-REOHCLBHSA-N |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Saccharomyces cerevisiae
(NCBI:txid4932)
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Source: yeast.sf.net
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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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 )
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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 )
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flour treatment agent
A food additive which is added to flour or dough to improve baking quality and/or colour.
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View more via ChEBI Ontology
(2R)-2-amino-3-mercaptopropanoic acid
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JCBN
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(2R)-2-amino-3-sulfanylpropanoic acid
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IUPAC
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(R)-2-amino-3-mercaptopropanoic acid
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NIST Chemistry WebBook
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C
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ChEBI
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Cys
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ChEBI
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CYSTEINE
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PDBeChem
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E 920
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ChEBI
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E-920
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ChEBI
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E920
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ChEBI
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FREE CYSTEINE
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PDBeChem
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L-2-Amino-3-mercaptopropionic acid
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KEGG COMPOUND
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L-Cystein
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ChEBI
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L-Cysteine
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KEGG COMPOUND
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L-Zystein
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ChEBI
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769
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DrugCentral
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C00001351
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KNApSAcK
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C00097
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KEGG COMPOUND
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CYS
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PDBeChem
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CYS
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MetaCyc
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Cysteine
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Wikipedia
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D00026
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KEGG DRUG
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DB00151
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DrugBank
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ECMDB00574
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ECMDB
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HMDB0000574
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HMDB
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YMDB00046
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YMDB
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View more database links |
1721408
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Reaxys Registry Number
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Reaxys
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49991
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Gmelin Registry Number
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Gmelin
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52-90-4
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CAS Registry Number
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KEGG COMPOUND
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52-90-4
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CAS Registry Number
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ChemIDplus
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52-90-4
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CAS Registry Number
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NIST Chemistry WebBook
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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] Macrophages are central players in immune response, manifesting divergent phenotypes to control inflammation and innate immunity through release of cytokines and other signaling factors. Recently, the focus on metabolism has been reemphasized as critical signaling and regulatory pathways of human pathophysiology, ranging from cancer to aging, often converge on metabolic responses. Here, we used genome-scale modeling and multi-omics (transcriptomics, proteomics, and metabolomics) analysis to assess metabolic features that are critical for macrophage activation. We constructed a genome-scale metabolic network for the RAW 264.7 cell line to determine metabolic modulators of activation. Metabolites well-known to be associated with immunoactivation (glucose and arginine) and immunosuppression (tryptophan and vitamin D3) were among the most critical effectors. Intracellular metabolic mechanisms were assessed, identifying a suppressive role for de-novo nucleotide synthesis. Finally, underlying metabolic mechanisms of macrophage activation are identified by analyzing multi-omic data obtained from LPS-stimulated RAW cells in the context of our flux-based predictions. Our study demonstrates metabolism's role in regulating activation may be greater than previously anticipated and elucidates underlying connections between activation and metabolic effectors. | 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] Elucidation of the 3D structure of histidine ammonia-lyase (HAL, EC 4.3.1.3) from Pseudomonas putida by X-ray crystallography revealed that the electrophilic prosthetic group at the active site is 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) [Schwede, T.F., Rétey, J., Schulz, G.E. (1999) Biochemistry, 38, 5355-5361]. To evaluate the importance of several amino-acid residues at the active site for substrate binding and catalysis, we mutated the following amino-acid codons in the HAL gene: R283, Y53, Y280, E414, Q277, F329, N195 and H83. Kinetic measurements with the overexpressed mutants showed that all mutations resulted in a decrease of catalytic activity. The mutants R283I, R283K and N195A were approximately 1640, 20 and 1000 times less active, respectively, compared to the single mutant C273A, into which all mutations were introduced. Mutants Y280F, F329A and Q277A exhibited approximately 55, 100 and 125 times lower activity, respectively. The greatest loss of activity shown was in the HAL mutants Y53F, E414Q, H83L and E414A, the last being more than 20 900-fold less active than the single mutant C273A, while H83L was 18 000-fold less active than mutant C273A. We propose that the carboxylate group of E414 plays an important role as a base in catalysis. To investigate a possible participation of active site amino acids in the formation of MIO, we used the chromophore formation upon treatment of HAL with l-cysteine and dioxygen at pH 10.5 as an indicator. All mutants, except F329A showed the formation of a 338-nm chromophore arising from a modified MIO group. The UV difference spectra of HAL mutant F329A with the MIO-free mutant S143A provide evidence for the presence of a MIO group in HAL mutant F329A also. For modelling of the substrate arrangement within the active site and protonation state of MIO, theoretical calculations were performed. | 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] Seven highly purified degradation products of penicillin G (PG) were examined with regard to their ability to cross-react allergically with PG. Guinea pig allergic contact dermatitis was employed as the test system. Three of these degradation products, D-benzylpenicillenic acid (BPE), D-penicillamine, and D-alpha-benzylpenicilloic acid were found to cross-react with PG and also to be capable of inducing delayed contact allergy in the guinea pig. BPE and PG cross-reacted with particularly intense reactions, and other immunologic experiments indicated that PG and BPE introduce identical allergic determinant groups into epidermal proteins. These experimental results were correlated with the results of previous studies concerning the degradation pathways of PG under physiological conditions in vitro, and the chemical reactivities of these degradation products. Based on these immunologic and chemical data, a schema is proposed which suggests the chemical pathways by which PG may react with epidermal proteins in vivo to form the penicillin antigen. The identity of the specific antigenic determinant groups of the penicillin antigen is suggested. The relationship between PG allergy of the contact dermatitis type in the guinea pig and PG allergy of the immediate type in man is discussed. |
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