title: Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis.
abstract: 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.
authors.affiliation: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
authors.forename: Kristin E
authors.initials: KE
authors.lastname: Burns
authors.forename: Sabine
authors.initials: S
authors.lastname: Baumgart
authors.forename: Pieter C
authors.initials: PC
authors.lastname: Dorrestein
authors.forename: Huili
authors.initials: H
authors.lastname: Zhai
authors.forename: Fred W
authors.initials: FW
authors.lastname: McLafferty
authors.forename: Tadhg P
authors.initials: TP
authors.lastname: Begley
mesh_terms: D003545:Cysteine / Q000096:biosynthesis* / Q000737:chemistry; D015394:Molecular Structure; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods
chemical_list: D003545:Cysteine