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