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4.4.1.13 |
| Description |
Cysteine-S-conjugate beta-lyase. |
| Catalyzed reaction |
RS-CH(2)-CH(NH(3)(+))COO(-) = RSH + NH(3) + pyruvate. |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
-!- R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitrobenzene. |
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Several PLP-dependent enzymes (mainly aminotransferases) show this activity, possibly as a side reaction.
In the public databases, sequences explicitly associated with this function also show kynurenine aminotransferase (EC 2.6.1.7) and glutamine-phenylpyruvate transaminase (EC 2.6.1.64) activities. These sequences have been included in the 2.6.1.7 family. |
| Organisms |
-Eubacteria -Plants -Fungi -Metazoa |
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| Links |
Enzyme (activities) 4.4.1.13
BRENDA (activities) 4.4.1.13
KEGG (pathways) 4.4.1.13
PLPMDB (PLP mutants) 4.4.1.13
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| References |
Cooper AJ, Pinto JT. (2006) Cysteine S-conjugate beta-lyases Amino Acids 30 1-15. Cooper, A. J.; Bruschi, S. A.; Iriarte, A.; Martinez-Carrion, M. (2002) Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions Biochem J 368 253-261. Kitamura, N.; Shimomura, N.; Iseki, J.; Honma, M.; Chiba, S.; Tahara, S.; Mizutani, J. (1997) Cysteine-S-conjugate beta-lyase activity and pyridoxal phosphate binding site of onion alliin lyase Biosci Biotechnol Biochem 61 1327-30. Alberati-Giani, D.; Malherbe, P.; Kohler, C.; Lang, G.; Kiefer, V.; Lahm, H. W.; Cesura, A. M. (1995) Cloning and characterization of a soluble kynurenine aminotransferase from rat brain: identity with kidney cysteine conjugate beta-lyase J Neurochem 64 1448-55. |
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| last changed |
2010/03/11 16:27 |
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