Site-site interactions and regulation of the activity of inorganic pyrophosphatases

Inorganic pyrophosphatases of baker's yeast and E. coli are oligomers built of chemically identical subunits. Both enzymes are active in the monomeric state. Each subunit has an active and an allosteric site linked by hetero- and homotropic interactions. These interactions are responsible for t...

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Bibliographic Details
Published in:Journal of molecular catalysis 1988-09, Vol.47 (2), p.307-314
Main Authors: Avaeva, Svetlana, Sklyankina, Vera, Baykov, Alexander, Nazarova, Tatjana
Format: Article
Language:English
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Summary:Inorganic pyrophosphatases of baker's yeast and E. coli are oligomers built of chemically identical subunits. Both enzymes are active in the monomeric state. Each subunit has an active and an allosteric site linked by hetero- and homotropic interactions. These interactions are responsible for the regulation of pyrophosphatase activity. Typical of these enzymes is the autocatalytic phosphorylation of the allosteric or active site and the regeneration of the initial enzyme via dephosphorylation in the process of the conformational change of the enzyme.
ISSN:0304-5102
DOI:10.1016/0304-5102(88)85055-7