EC Number |
General Information |
Reference |
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2.7.7.64 | evolution |
phylogenetic analysis |
721524 |
2.7.7.64 | malfunction |
A knock-out of the USP gene results in non-fertile pollen. Mutant plants show an arabinose reduction in the cell wall, and accumulate mainly two sugars, arabinose and xylose, in the cytoplasm |
726176 |
2.7.7.64 | malfunction |
inactivation of the two parasite diphosphorylases UGP and USP, results in parasite death |
761959 |
2.7.7.64 | metabolism |
Leishmania parasites possess a UDP-sugar pyrophosphorylase (USP), which has broad substrate specificity and is involved in monosaccharide salvage |
761959 |
2.7.7.64 | metabolism |
the enzyme, likely involved in monosaccharide salvage, preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate |
722975 |
2.7.7.64 | metabolism |
UDP-sugar pyrophosphorylases are involved in the plant salvage pathways |
761567 |
2.7.7.64 | more |
active site conformations of apoenzyme and ligand-bound enzyme, substrate binding structures, structure-function analysis, modeling, overview |
722975 |
2.7.7.64 | physiological function |
enzyme is able to complement an Escherichia coli GalU mutant |
738819 |
2.7.7.64 | physiological function |
gene silencing of USP by miRNA causes a concomitant reduction of USP and of glucuronokinase activity presumably to prevent the accumulation of sugar-1-phosphates interfering with normal metabolism and depleting the phosphate pool of the cell |
739372 |
2.7.7.64 | physiological function |
Leishmania parasites express a UDP-sugar pyrophosphorylase (USP) responsible for monosaccharides salvage that is able to generate both UDP-Gal and UDP-Glc. In vitro, Leishmania USP preferentially uses UTP as a nucleotide donor, and can activate a variety of sugar-1-phosphates. The enzyme is most active with galactose 1-phosphate and glucose 1-phosphate, with a slight preference for the former, but it cannot activate N-acetylated sugars. UDP-sugar-producing diphosphorylases catalyze reversible reactions, require magnesium for catalysis, and act through an ordered sequential Bi-Bi reaction mechanism. In the forward reaction, UTP binds before the sugar 1-phosphate, and after catalysis, inorganic diphosphate is released before the UDP-sugar |
761959 |