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