Journal Article

PreJuSER-18052

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase

Alderwick, L. J. ; Lloyd, G. S. ; Lloyd, A. J. ; Lovering, A. L. ; Eggeling, L.FZJ* ; Besra, G. S.

2011
Oxford Univ. Press Oxford

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Please use a persistent id in citations: doi:10.1093/glycob/ewq173

Abstract: Mycobacterium tuberculosis arabinogalactan (AG) is an essential cell wall component. It provides a molecular framework serving to connect peptidoglycan to the outer mycolic acid layer. The biosynthesis of the arabinan domains of AG and lipoarabinomannan (LAM) occurs via a combination of membrane bound arabinofuranosyltransferases, all of which utilize decaprenol-1-monophosphorabinose as a substrate. The source of arabinose ultimately destined for deposition into cell wall AG or LAM originates exclusively from phosphoribosyl-1-pyrophosphate (pRpp), a central metabolite which is also required for other essential metabolic processes, such as de novo purine and pyrimidine biosyntheses. In M. tuberculosis, a single pRpp synthetase enzyme (Mt-PrsA) is solely responsible for the generation of pRpp, by catalyzing the transfer of pyrophosphate from ATP to the C1 hydroxyl position of ribose-5-phosphate. Here, we report a detailed biochemical and biophysical study of Mt-PrsA, which exhibits the most rapid enzyme kinetics reported for a pRpp synthetase.

Keyword(s): J ; arabinan (auto) ; cell wall (auto) ; Mycobacteria (auto) ; phosphoribosylpyrophosphate (auto) ; polysaccharides (auto)

Note: G.S.B. acknowledges support in the form of a Personal Research Chair from Mr. James Bardrick, Royal Society Wolfson Research Merit Award, as a former Lister Institute-Jenner Research Fellow, the Medical Research Council and The Wellcome Trust (081569/Z/06/Z).

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Contributing Institute(s):

1. Biotechnologie 1 (IBT-1)

Research Program(s):

1. Biotechnologie (PBT)

Appears in the scientific report 2011

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