| Entry |
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| Name |
cysteine-S-conjugate beta-lyase;
cysteine conjugate beta-lyase;
glutamine transaminase K/cysteine conjugate beta-lyase;
L-cysteine-S-conjugate thiol-lyase (deaminating);
cystathionine beta-lyase;
beta-cystathionase;
cystine lyase;
cystathionine L-homocysteine-lyase (deaminating);
L-cystathionine L-homocysteine-lyase (deaminating);
CBL;
S-alkylcysteine lyase;
S-alkylcysteinase;
alkylcysteine lyase;
S-alkyl-L-cysteine sulfoxide lyase;
S-alkyl-L-cysteine lyase;
S-alkyl-L-cysteinase;
alkyl cysteine lyase;
S-alkyl-L-cysteine alkylthiol-lyase (deaminating)
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| Class |
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
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| Sysname |
L-cysteine-S-conjugate thiol-lyase (deaminating; 2-aminoprop-2-enoate-forming)
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| Reaction(IUBMB) |
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate (overall reaction) [RN: R03528];
(1a) an L-cysteine-S-conjugate = a thiol + 2-aminoprop-2-enoate;
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous);
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
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| Reaction(KEGG) |
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| Substrate |
L-cysteine-S-conjugate [CPD: C02882];
H2O [CPD: C00001];
2-aminoprop-2-enoate [CPD: C02218];
2-iminopropanoate [CPD: C20904]
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| Product |
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| Comment |
A pyridoxal-phosphate protein. The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases.
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| History |
EC 4.4.1.13 created 1981, modified 2018 (EC 4.4.1.6 created 1965, deleted 1972, reinstated 1976, incorporated 2018) (EC 4.4.1.8 created 1972, incorporated 2018)
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| Pathway |
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| Orthology |
| K00816 | kynurenine---oxoglutarate transaminase / cysteine-S-conjugate beta-lyase / glutamine---phenylpyruvate transaminase |
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| Genes |
» show all
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| Reference |
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| Authors |
FLAVIN M, SLAUGHTER C. |
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| Title |
CYSTATHIONINE CLEAVAGE ENZYMES OF NEUROSPORA. |
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| Journal |
J Biol Chem 239:2212-9 (1964) |
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| Reference |
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| Authors |
Tateishi M, Suzuki S, Shimizu H. |
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| Title |
Cysteine conjugate beta-lyase in rat liver. A novel enzyme catalyzing formation of thiol-containing metabolites of drugs. |
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| Journal |
J Biol Chem 253:8854-9 (1978) |
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| Reference |
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| Authors |
Stevens JL |
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| Title |
Isolation and characterization of a rat liver enzyme with both cysteine conjugate beta-lyase and kynureninase activity. |
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| Journal |
J Biol Chem 260:7945-50 (1985) |
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| Reference |
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| Authors |
Stevens JL, Robbins JD, Byrd RA |
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| Title |
A purified cysteine conjugate beta-lyase from rat kidney cytosol. Requirement for an alpha-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K. |
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| Journal |
J Biol Chem 261:15529-37 (1986) |
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| Reference |
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| Authors |
Gaskin PJ, Adcock HJ, Buckberry LD, Teesdale-Spittle PH, Shaw PN |
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| Title |
The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes. |
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| Journal |
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| Reference |
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| Authors |
Cooper AJ, Bruschi SA, Iriarte A, Martinez-Carrion M |
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| Title |
Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions. |
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| Journal |
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| Reference |
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| Authors |
Cooper AJ, Bruschi SA, Conway M, Hutson SM |
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| Title |
Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate beta-lyases, but turnover leads to inactivation. |
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| Journal |
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| Reference |
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| Authors |
Natsch A, Schmid J, Flachsmann F |
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| Title |
Identification of odoriferous sulfanylalkanols in human axilla secretions and their formation through cleavage of cysteine precursors by a C-S lyase isolated from axilla bacteria. |
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| Journal |
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| Reference |
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| Authors |
Cooper AJ, Pinto JT |
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| Title |
Cysteine S-conjugate beta-lyases. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 4.4.1.13 |
| ExPASy - ENZYME nomenclature database: | 4.4.1.13 |
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