Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 91, Issue 1, Pages 47-61Publisher
SPRINGER
DOI: 10.1007/s00253-011-3336-x
Keywords
Cysteine desulfurase; Sulfur transfer; Sulfur-containing biofactors; Biosynthetic pathways; A persulfide intermediate
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Funding
- Grants-in-Aid for Scientific Research [23380060] Funding Source: KAKEN
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Cysteine desulfurases are pyridoxal 5'-phosphate-dependent homodimeric enzymes that catalyze 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. The enzymes are capable of donating the persulfide sulfur atoms to a variety of biosynthetic pathways for sulfur-containing biofactors, such as iron-sulfur clusters, thiamin, transfer RNA thionucleosides, biotin, and lipoic acid. The enormous advances in biochemical and structural studies of these biosynthetic pathways over the past decades provide an opportunity for detailed understanding of the nature of the excellent sulfur transfer mechanism of cysteine desulfurases.
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