Bacterial cysteine desulfurases: their function and mechanisms View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-10

AUTHORS

H. Mihara, N. Esaki

ABSTRACT

Cysteine desulfurase is a pyridoxal 5'-phosphate (PLP)-dependent homodimeric enzyme that catalyzes the conversion of L-cysteine to L-alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue. Increased evidence for the functions of cysteine desulfurases has revealed their important roles in the biosyntheses of Fe-S clusters, thiamine, thionucleosides in tRNA, biotin, lipoic acid, molybdopterin, and NAD. The enzymes are also proposed to be involved in cellular iron homeostasis and in the biosynthesis of selenoproteins. The mechanisms for sulfur mobilization mediated by cysteine desulfurases are as yet unknown, but enzymes capable of providing a variety of biosynthetic pathways for sulfur/selenium-containing biomolecules are probably applicable to the production of cofactors and the bioconversion of useful compounds. More... »

PAGES

12-23

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00253-002-1107-4

DOI

http://dx.doi.org/10.1007/s00253-002-1107-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005016660

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12382038


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