Cysteine Dealkylation in Bacillus subtilis by a Novel Flavin-Dependent Monooxygenase. Academic Article uri icon

abstract

  • In this paper, we describe the biochemical reconstitution of a cysteine salvage pathway and the biochemical characterization of each of the five enzymes involved. The salvage begins with amine acetylation of S-alkylcysteine, followed by thioether oxidation. The C-S bond of the resulting sulfoxide is cleaved using a new flavoenzyme catalytic motif to give N-acetylcysteine sulfenic acid. This is then reduced to the thiol and deacetylated to complete the salvage pathway. We propose that this pathway is important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.

published proceedings

  • Biochemistry

altmetric score

  • 1.75

author list (cited authors)

  • Hazra, S., Bhandari, D. M., Krishnamoorthy, K., Sekowska, A., Danchin, A., & Begley, T. P.

citation count

  • 3

complete list of authors

  • Hazra, Sohan||Bhandari, Dhananjay M||Krishnamoorthy, Kalyanaraman||Sekowska, Agnieszka||Danchin, Antoine||Begley, Tadhg P

publication date

  • January 2022