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- W2009134768 abstract "UDP-Glucuronate, formed through dehydrogenation of UDP-glucose and itself decarboxy-lated to make UDP-xylose, is the presumed donor for the glucuronyl side-groups in biosynthesis of the capsular polysaccharide in Cryptococcus neoformans. A specific radiochromatographic assay for UDP-glucose dehydrogenase shows that the enzyme is present in the cytosol. The enzyme is very labile but is stabilized by 25% glycerol. The enzyme is inhibited strongly by NADH (Ki.NADH = Km.NAD = 0.1 to 0.2 mm). It is also inhibited competitively by UDP-xylose (Ki = 0.3 mm). These results suggest that the rate of production of the capsular precursor, UDP-glucuronate, is controlled by the intracellular concentrations of an end product. UDP-xylose, and of a direct product, NADH. Capsule mutants have been screened for activity of this enzyme but none is clearly deficient." @default.
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- W2009134768 date "1987-01-01" @default.
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- W2009134768 title "Cryptococcal UDP-glucose dehydrogenase: enzymic control of capsular biosynthesis" @default.
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- W2009134768 doi "https://doi.org/10.1080/02681218780000201" @default.
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