Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis. Academic Article uri icon


  • A new pathway for cysteine biosynthesis has been elucidated in Mycobacterium tuberculosis. This pathway involves a protein-bound thiocarboxylate (CysO-SH) as the sulfide donor, similar to thiamin biosynthesis. Cysteine synthase M (CysM) catalyzes the addition of cysteine to the carboxy terminus of the protein-bound thiocarboxylate to generate a CysO-cysteine adduct. A protease, Mec+, hydrolyzes the CysO-cysteine adduct to release cysteine and regenerate CysO. Mec+ contains a JAMM motif, and this work provides the first functional characterization of the JAMM motif in prokaryotes. MoeZ, a paralogue of ThiF, has been shown to transfer sulfur onto CysO.

published proceedings

  • J Am Chem Soc

altmetric score

  • 9

author list (cited authors)

  • Burns, K. E., Baumgart, S., Dorrestein, P. C., Zhai, H., McLafferty, F. W., & Begley, T. P.

citation count

  • 77

complete list of authors

  • Burns, Kristin E||Baumgart, Sabine||Dorrestein, Pieter C||Zhai, Huili||McLafferty, Fred W||Begley, Tadhg P

publication date

  • August 2005