Bacterial cysteine desulfurases: their function and mechanisms

@article{Mihara2002BacterialCD,
  title={Bacterial cysteine desulfurases: their function and mechanisms},
  author={H. Mihara and N. Esaki},
  journal={Applied Microbiology and Biotechnology},
  year={2002},
  volume={60},
  pages={12-23}
}
  • H. Mihara, N. Esaki
  • Published 2002
  • Chemistry, Medicine
  • Applied Microbiology and Biotechnology
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… Expand
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