B6db activities : 4_4_1

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	4.4.1.25
Description	L-cysteate sulfo-lyase
Alternative names	L-cysteate sulfo-lyase (deaminating); CuyA.
Catalyzed reaction	L-cysteate + H2O = pyruvate + bisulfite + NH3
Cofactor	Pyridoxal-phosphate.
Comments	A pyridoxal-phosphate protein. D-Cysteine can also act as a substrate, but more slowly. It is converted into pyruvate, sulfide and NH3. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.
	In the original paper (Denger et al. 2006 Biochem J. 394 657-64) the enzyme was called L-cysteate sulfo-lyase. However, in a subsequent paper (Denger et al. 2009 J Bacteriol 191 5648-56) the same enzyme was termed (S)-cysteate sulfo-lyase. (S)-cysteate should correspond to the D- (not L) form of the amino acid. This would agree with the activity shown by the Silicibater enzyme towards D-cysteine.
Organisms	-Eubacteria
Family	4.4.1.25 (0)

Links	Enzyme (activities) 4.4.1.25 BRENDA (activities) 4.4.1.25 KEGG (pathways) 4.4.1.25 PLPMDB (PLP mutants) 4.4.1.25

References	Denger K, Mayer J, Buhmann M, Weinitschke S, Smits TH, Cook AM. (2009) Bifurcated degradative pathway of 3-sulfolactate in Roseovarius nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate sulfolyase J Bacteriol 191 5648-56. Denger, K.; Smits, T.H.; Cook, A.M. (2006) L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T) Biochem J. 394 657-64. Articles on 4.4.1.25

last changed	2016/10/06 17:22

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