The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: Structural studies and mechanistic implications




Tuominen V, Heikinheimo P, Kajander T, Torkkel T, Hyytia T, Kapyla J, Lahti R, Cooperman BS, Goldman A

PublisherACADEMIC PRESS LTD

1998

JOURNAL OF MOLECULAR BIOLOGY

J MOL BIOL

284

5

1565

1580

16

0022-2836

DOIhttps://doi.org/10.1006/jmbi.1998.2266



These new structures, together with parallel functional studies measuring catalytic efficiency and ligand (metal ion, PPi and P-i) binding, provide strong evidence against a proposed mechanism in which Wat1 is considered unimportant for hydrolysis. They thus support the notion that PPase shares mechanistic similarity with the "two-metal ion" mechanism of polymerases. (C) 1998 Academic Press.



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