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Effectory Site in Escherichia Coli Inorganic Pyrophosphatase Is Revealed Upon Mutation at the Intertrimeric Interface

Effectory Site in Escherichia Coli Inorganic Pyrophosphatase Is Revealed Upon Mutation at the Intertrimeric Interface

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

IUBMB Life. 2003 Jan;55(1):37-41.

PMID: 12716061

Abstract:

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 a subsite is confirmed by the finding that the free form of methylenediphosphonate activates MgPPi hydrolysis though its magnesium complex is a competitive inhibitor. The Asp26Ala variant is the first example of hexameric E-PPase demonstrated to have an activatory subsite.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9024822	Pyrophosphatase, Inorganic from Escherichia coli		9024-82-2	Price

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