Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors

Appl Microbiol Biotechnol. 2011 Jul;91(1):47-61. doi: 10.1007/s00253-011-3336-x. Epub 2011 May 21.


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.

Publication types

  • Review

MeSH terms

  • Bacteria / enzymology*
  • Bacteria / genetics
  • Bacteria / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Biosynthetic Pathways*
  • Carbon-Sulfur Lyases / genetics
  • Carbon-Sulfur Lyases / metabolism*
  • RNA, Bacterial / genetics
  • RNA, Bacterial / metabolism
  • Sulfur / metabolism*


  • Bacterial Proteins
  • RNA, Bacterial
  • Sulfur
  • Carbon-Sulfur Lyases
  • cysteine desulfurase