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Article

Effectory site in Escherichia coli inorganic pyrophosphatase is revealed upon mutation at the intertrimeric interface.

IUBMB life - 1 Jan 2003

Sitnik Tatyana S, Vainonen Julia P, Rodina Elena V, Nazarova Tatyana I, Kurilova Svetlana A, Vorobyeva Natalya N, Avaeva Svetlana M

Abstract excerpt

Escherichia coli inorganic pyrophosphatase (E-PPase) is a homohexamer formed from two trimers related by a two-fold axis. The residue Asp26 participates in intertrimeric contacts. Kinetics of MgPPi hydrolysis by a mutant Asp26Ala E-PPase is found to not obey Michaelis-Menten equation but can be described within the scheme of activation of hydrolysis by a free PPi binding at an effectory subsite. Existence of such...

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PMID: 12716061
DOI: 10.1080/1521654031000072139

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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