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Oxford University Press, Glycobiology, 4(21), p. 410-425, 2010

DOI: 10.1093/glycob/cwq173

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Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase

Journal article published in 2010 by Luke J. Alderwick, Georgina S. Lloyd, Adrian J. Lloyd, Andrew L. Lovering, Lothar Eggeling, Gurdyal S. Besra ORCID
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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 utilise decaprenol-1-monophosphorabinose as a substrate (DPA). 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 pyrimidne biosynthesis. In M. tuberculosis, a single pRpp synthetase enzyme (Mt-PrsA) is soley responsible for the generation of pRpp, by catalysing 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.