A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: Structural studies and mechanistic implications
Tekijät: Tuominen V, Heikinheimo P, Kajander T, Torkkel T, Hyytia T, Kapyla J, Lahti R, Cooperman BS, Goldman A
Kustantaja: ACADEMIC PRESS LTD
Julkaisuvuosi: 1998
Tietokannassa oleva lehden nimi: JOURNAL OF MOLECULAR BIOLOGY
Lehden akronyymi: J MOL BIOL
Vuosikerta: 284
Numero: 5
Aloitussivu: 1565
Lopetussivu: 1580
Sivujen määrä: 16
ISSN: 0022-2836
DOI: https://doi.org/10.1006/jmbi.1998.2266
Tiivistelmä
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.
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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