Uridine phosphorylase from Escherichia coli. Kinetic properties and mechanism.
Type I and Type II uridine phosphorylases (uridine: orthophosphate ribosyltransferase EC 2.4.2.3) are distinguished by their pH optima (Krenitsky et al. (1965) J. Biol. Chem. 240, 1281-1286). A Type I enzyme was partially purified from Escherichia coli. The crossing pattern of the initial velocity analysis indicated that the catalytic mechanism involved the sequential addition of substrates to the enzyme. Product inhibition by uracil or by ribose 1-phosphate was linear competitive with uridine or with concentrations of phosphate below 3 mM. This indicated that the sequence of substrate addition was random rather than ordered. At concentrations of phosphate above 3 mM, product inhibition by uracil was complex. The random mechanism of this Type I enzyme contrasts with the ordered mechanism of a Type II enzyme from rat liver (Kraut, A. and Yamada, E.W. (1971) J. Biol. Chem. 246, 2021-2030).
D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D010430:Pentosyltransferases / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology; D014498:Uracil / Q000494:pharmacology; D014529:Uridine / Q000494:pharmacology; D014543:Uridine Phosphorylase / Q000302:isolation & purification / Q000378:metabolism*
D010710:Phosphates; D014498:Uracil; D010430:Pentosyltransferases; D014543:Uridine Phosphorylase; D014529:Uridine