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

Applied Microbiology and Biotechnology volume 91, pages 47–61 (2011)Cite this article

Abstract

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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Affiliations

  1. Institute for Chemical Research, Kyoto University, Uji, Kyoto, 611-0011, Japan

    Ryota Hidese & Nobuyoshi Esaki

  2. Department of Biotechnology, Institute of Science and Engineering, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525–8577, Japan

    Hisaaki Mihara

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  1. Ryota Hidese
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Hidese, R., Mihara, H. & Esaki, N. Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors. Appl Microbiol Biotechnol 91, 47–61 (2011). https://doi.org/10.1007/s00253-011-3336-x

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  • DOI: https://doi.org/10.1007/s00253-011-3336-x

Keywords

  • Cysteine desulfurase
  • Sulfur transfer
  • Sulfur-containing biofactors
  • Biosynthetic pathways
  • A persulfide intermediate