Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis.
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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.
author list (cited authors)
Burns, K. E., Baumgart, S., Dorrestein, P. C., Zhai, H., McLafferty, F. W., & Begley, T. P.
complete list of authors
Burns, Kristin E||Baumgart, Sabine||Dorrestein, Pieter C||Zhai, Huili||McLafferty, Fred W||Begley, Tadhg P