A1 Refereed original research article in a scientific journal

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



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

Publisher: ACADEMIC PRESS LTD

Publication year: 1998

Journal name in source: JOURNAL OF MOLECULAR BIOLOGY

Journal acronym: J MOL BIOL

Volume: 284

Issue: 5

First page : 1565

Last page: 1580

Number of pages: 16

ISSN: 0022-2836

DOI: https://doi.org/10.1006/jmbi.1998.2266


Abstract
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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