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

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

• Begley, Tadhg

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

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Cysteine
• Molecular Structure
• Mycobacterium Tuberculosis
• Spectrometry, Mass, Electrospray Ionization

PubMed Central ID

• 16104727

Digital Object Identifier (DOI)

• 10.1021/ja053476x

start page

• 11602

end page

• 11603

volume

• 127

issue

• 33

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja053476x

user-defined tag

• 3 Good Health and Well-Being