Evidence that catalysis by yeast inorganic pyrophosphatase proceeds by direct phosphoryl transfer to water and not via a phosphoryl enzyme intermediate.
作者： Marcel A. Gonzalez , Martin R. Webb , Katherine M. Welsh , Barry S. Cooperman
DOI: 10.1021/BI00300A002
关键词:
摘要: In this work, we show that adenosine 5'-O-(3-thiotriphosphate) (ATP gamma S) is a substrate for yeast inorganic pyrophosphatase (PPase) (EC 3.6.1.1) and further, using chirally labeled [gamma-17O,18O]ATP S, enzyme-catalyzed hydrolysis to produce chiral thio[17O,18O]phosphate proceeds with inversion of configuration. Both the synthesis ATP S determination thiophosphate configuration were carried out as described by Webb [Webb, M. R. (1982) Methods Enzymol. 87, 301-316]. We also in single turnover experiment performed H2(18)O 1 mol each 18O16O3P 16O4P produced per pyrophosphate hydrolyzed, strong indication oxygen uptake form phosphate on PPase catalysis comes directly from H2O. These two results provide evidence conclusion catalyzes via single-step direct phosphoryl transfer water does not involve formation phosphorylated enzyme intermediate.
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