ExplorEnz: EC 4.4.1.28

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4.4.1.28

Accepted name:

L-cysteine desulfidase

Reaction:

L-cysteine + H₂O = sulfide + NH₃ + pyruvate (overall reaction)
(1a) L-cysteine = 2-aminoprop-2-enoate + sulfide
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H₂O = pyruvate + NH₃ (spontaneous)

Other name(s):

L-cysteine desulfhydrase

Systematic name:

L-cysteine sulfide-lyase (deaminating; pyruvate-forming)

Comments:

The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1, cystathionine γ-lyase). It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The same reaction can also be catalysed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1, cystathionine γ-lyase).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Tchong, S.I., Xu, H. and White, R.H. L-Cysteine desulfidase: an [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide. Biochemistry 44 (2005) 1659–1670. [DOI] [PMID: 15683250]

[EC 4.4.1.28 created 2014]