EC 2.8.1.7 - Cysteine desulfurase

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IntEnz Enzyme Nomenclature
EC 2.8.1.7

Names

Accepted name:
cysteine desulfurase
Other names:
IscS
NIFS
NifS
SufS
cysteine desulfurylase
Systematic name:
L-cysteine:acceptor sulfurtransferase

Reactions

Cofactor

Comments:

A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) [2]. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0031071
UniProtKB/Swiss-Prot: (298) [show] [UniProt]

References

  1. Zheng, L.M., White, R.H., Cash, V.L., Jack, R.F. and Dean, D.R.
    Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
    Proc. Natl. Acad. Sci. USA 90: 2754-2758 (1993). [PMID: 8464885]
  2. Mihara, H. and Esaki, N.
    Bacterial cysteine desulfurases: Their function and mechanisms.
    Appl. Microbiol. Biotechnol. 60: 12-23 (2002). [PMID: 12382038]
  3. Frazzon, J. and Dean, D.R.
    Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry.
    Curr. Opin. Chem. Biol. 7: 166-173 (2003). [PMID: 12714048]

[EC 2.8.1.7 created 2003, modified 2011]