[Methylpyrophosphate, the simplext organic substrate of yeast inorganic phyrophosphatase].
The interaction between yeast inorganic pyrophosphatase and the simplest organic substrate, methylpyrophosphate, was studied. Methylpyrophosphate hydrolysis occurred most intensively in the presence of Zn2+ less intensively in the presence of CO2+ and Mn2+ and did not occur at all in the presence of Mg2+. The complex convertible into reaction products contains two Zn2+ and one molecule of zinc methylpyrophosphate per one active center. The activator metal ions are linked with pyrophosphatase consecutively; each of the two enzyme forms produced can bind to the substrate. The values of the maximal velocity and the constants of the substrate binding to the pyrophosphatase were calculated.
D001665:Binding Sites; D002413:Cations, Divalent; D011756:Diphosphates; D043564:Inorganic Pyrophosphatase; D007700:Kinetics; D011755:Pyrophosphatases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D002413:Cations, Divalent; D011756:Diphosphates; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase
Metilpirofosfat--prosteĭshiĭ organicheskiĭ substrat neorganicheskoĭ pirofosfatazy iz drozhzheĭ.