A1 Refereed original research article in a scientific journal

The structural basis for pyrophosphatase catalysis




AuthorsHeikinheimo P, Lehtonen J, Baykov A, Lahti R, Cooperman BS, Goldman A

PublisherCURRENT BIOLOGY LTD

Publication year1996

JournalStructure

Journal name in sourceSTRUCTURE

Journal acronymSTRUCTURE

Volume4

Issue12

First page 1491

Last page1508

Number of pages18

ISSN0969-2126

DOIhttps://doi.org/10.1016/S0969-2126(96)00155-4(external)


Abstract
Conclusions: Our structure-based model of the PPase mechanism posits that the nucleophile is the hydroxide ion mentioned above. This aspect of the mechanism is formally analogous to the 'two-metal ion' mechanism of alkaline phosphatase, exonucleases and polymerases. A third metal ion coordinates another water molecule that is probably the required general acid. Extensive Lewis acid coordination and hydrogen bonds provide charge shielding of the electrophile and lower the pK(a) of the leaving group. This 'three-metal ion' mechanism is in detail different from that of other phosphoryl transfer enzymes, presumably reflecting how ancient the reaction is.



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