Escherichia coli K-12 substr. MG1655 Compound: L-cysteine

Abbrev Name: cys

Synonyms: C, carbocysteine, cysteine, Cys, L-cys

Superclasses: an amino acid or its derivative an amino acid a non-polar amino acid
an amino acid or its derivative an amino acid a polar amino acid an uncharged polar amino acid
an amino acid or its derivative an amino acid an alpha amino acid a standard alpha amino acid
an amino acid or its derivative an amino acid an L-amino acid

Chemical Formula: C3H7NO2S

Molecular Weight: 121.15 Daltons

Monoisotopic Molecular Weight: 121.01974916409999 Daltons

L-cysteine compound structure

SMILES: C(S)C(C(=O)[O-])[N+]

InChI: InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1


Unification Links: CAS:52-90-4 , CAS:4371-52-2 , ChEBI:35235 , HMDB:HMDB00574 , IAF1260:33843 , KEGG:C00097 , KNApSAcK:C00001351 , MetaboLights:MTBLC35235 , PubChem:6419722

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -81.21

Reactions known to consume the compound:

coenzyme A biosynthesis I :
(R)-4'-phosphopantothenate + L-cysteine + CTP → CMP + R-4'-phosphopantothenoyl-L-cysteine + diphosphate + H+

glutathione biosynthesis :
L-cysteine + L-glutamate + ATP → γ-L-glutamyl-L-cysteine + ADP + phosphate + H+

hydrogen sulfide biosynthesis I :
2-oxoglutarate + L-cysteine → L-glutamate + 3-mercaptopyruvate

L-alanine biosynthesis III , molybdenum cofactor biosynthesis , thiazole biosynthesis I (E. coli) :
an [L-cysteine desulfurase]-L-cysteine + L-cysteine → an [L-cysteine desulfurase] L-cysteine persulfide + L-alanine

L-cysteine degradation II :
L-cysteine → 2-aminoprop-2-enoate + hydrogen sulfide + H+

L-methionine biosynthesis I :
L-cysteine + O-succinyl-L-homoserine → succinate + L-cystathionine + H+

tRNA charging :
a tRNAcys + L-cysteine + ATP + H+ → an L-cysteinyl-[tRNAcys] + AMP + diphosphate

Not in pathways:
L-cysteine + an unsulfurated [sulfur carrier] → L-alanine + a sulfurated [sulfur carrier]
L-cysteine + H2O → pyruvate + ammonium + hydrogen sulfide

Reactions known to produce the compound:

Not in pathways:
L-cysteinyl-glycine + H2O → L-cysteine + glycine
a reduced thioredoxin + L-cystine → an oxidized thioredoxin + 2 L-cysteine

Not in pathways:
a peptide with an N-terminal X-L-proline + H2O → a standard α amino acid + a peptide with an N-terminal L-proline + H+
a peptide + H2O → a standard α amino acid + a peptide
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a standard α amino acid + a peptide
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid
a dipetide with an N-terminal L-aspartate + H2O → L-aspartate + a standard α amino acid
a tripeptide + H2O → a dipeptide + a standard α amino acid
a dipeptide with proline at the C-terminal + H2O → L-proline + a standard α amino acid
a dipeptide + H2O → 2 a standard α amino acid

Not in pathways:
a polypeptide + H2O → a polypeptide + an L-amino acid

Reactions known to both consume and produce the compound:

L-cysteine biosynthesis I :
O-acetyl-L-serine + hydrogen sulfide ↔ L-cysteine + acetate + H+

In Reactions of unknown directionality:

Not in pathways:
L-cystine + 2 glutathione = glutathione disulfide + 2 L-cysteine
L-cystein desulfurase + L-cysteine = an S-sulfanyl-[L-cysteine desulfurase] + L-alanine
a ThiI sulfur-carrier protein + L-cysteine = an S-sulfanyl-[ThiI sulfur-carrier protein] + L-alanine
DsbAoxidised[periplasmic space] + 2 L-cysteine[periplasmic space] = L-cystine[periplasmic space] + DsbAreduced[periplasmic space]
'activated' tRNA + L-cysteine = L-serine + tRNA containing a thionucleotide
ThiS-COAMP + L-cysteine = ThiS-COSH + L-alanine + AMP

Not in pathways:
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + a standard α amino acid

Not in pathways:
a 5-L-glutamyl-[peptide][periplasmic space] + an amino acid[periplasmic space] = a 5-L-glutamyl-amino acid[periplasmic space] + a peptide[periplasmic space]

In Transport reactions:
L-cysteine[cytosol] + ATP + H2O → L-cysteine[periplasmic space] + ADP + phosphate + H+ ,
L-cysteine[periplasmic space] + ATP + H2O → L-cysteine[cytosol] + ADP + phosphate + H+ ,
L-cysteine[cytosol]L-cysteine[periplasmic space] ,
an L-amino acid[cytosol]an L-amino acid[periplasmic space]

Enzymes activated by L-cysteine, sorted by the type of activation, are:

Activator (Mechanism unknown) of: phosphoglucomutase [Joshi64]

Enzymes inhibited by L-cysteine, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: cystathionine-β-lyase [Dwivedi82] , serine acetyltransferase [Kredich66] , homoserine kinase [Theze74, Burr76, Comment 1]

Inhibitor (Mechanism unknown) of: L-cystine ABC transporter [Deutch14] , alkaline phosphatase [Malamy64] , L-serine deaminase [Cicchillo04] , D-glucuronate isomerase [Ashwell60] , D-galacturonate isomerase [Ashwell60] , alkaline phosphatase [Malamy64] , 8-amino-7-oxononanoate synthase [Eisenberg68, Eisenberg73] , 2-amino-3-ketobutyrate CoA ligase [Mukherjee87]

Inhibitor (Other types) of: threonine deaminase [Harris81]

This compound has been characterized as an alternative substrate of the following enzymes: cysteine sulfinate desulfinase , selenocysteine lyase

In Growth Media: Neidhardt EZ rich defined medium , PMA sulfur source test + cys , PMA nitrogen source test + cys


Ashwell60: Ashwell G, Wahba AJ, Hickman J (1960). "Uronic acid metabolism in bacteria. I. Purification and properties of uronic acid isomerase in Escherichia coli." J Biol Chem 1960;235(6):1559-1565. PMID: 13794771

Burr76: Burr B, Walker J, Truffa-Bachi P, Cohen GN (1976). "Homoserine kinase from Escherichia coli K12." Eur J Biochem 1976;62(3);519-26. PMID: 177283

Cicchillo04: Cicchillo RM, Baker MA, Schnitzer EJ, Newman EB, Krebs C, Booker SJ (2004). "Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis." J Biol Chem 279(31);32418-25. PMID: 15155761

Deutch14: Deutch CE, Spahija I, Wagner CE (2014). "Susceptibility of Escherichia coli to the toxic L-proline analogue L-selenaproline is dependent on two L-cystine transport systems." J Appl Microbiol. PMID: 25139244

Dwivedi82: Dwivedi CM, Ragin RC, Uren JR (1982). "Cloning, purification, and characterization of beta-cystathionase from Escherichia coli." Biochemistry 1982;21(13);3064-9. PMID: 7049234

Eisenberg68: Eisenberg MA, Star C (1968). "Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in cell-free extracts of Escherichia coli biotin auxotrophs." J Bacteriol 1968;96(4);1291-7. PMID: 4879561

Eisenberg73: Eisenberg MA (1973). "Biotin: biogenesis, transport, and their regulation." Adv Enzymol Relat Areas Mol Biol 1973;38;317-72. PMID: 4598072

Harris81: Harris CL (1981). "Cysteine and growth inhibition of Escherichia coli: threonine deaminase as the target enzyme." J Bacteriol 145(2);1031-5. PMID: 7007336

Joshi64: Joshi JG, Handler P (1964). "Phosphoglucomutase. I. Purification and properties of phosphoglucomutase from Escherichia coli." J. Biol. Chem. 239:2741-2751. PMID: 14216423

Kredich66: Kredich NM, Tomkins GM (1966). "The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium." J Biol Chem 1966;241(21);4955-65. PMID: 5332668

Malamy64: Malamy, MH, Horecker, BL "Purification and Crystallization of the Alkaline Phosphatase of Escherichia coli." Biochemistry 3:1893-1897 (1964).

Mukherjee87: Mukherjee JJ, Dekker EE (1987). "Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme." J Biol Chem 1987;262(30);14441-7. PMID: 3117785

Theze74: Theze J, Kleidman L, St Girons I (1974). "Homoserine kinase from Escherichia coli K-12: properties, inhibition by L-threonine, and regulation of biosynthesis." J Bacteriol 1974;118(2);577-81. PMID: 4364023

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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