PMID:12716061
| Citation |
Sitnik, TS, Vainonen, JP, Rodina, EV, Nazarova, TI, Kurilova, SA, Vorobyeva, NN and Avaeva, SM (2003) Effectory site in Escherichia coli inorganic pyrophosphatase is revealed upon mutation at the intertrimeric interface. IUBMB Life 55:37-41 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1080/1521654031000072139 |
| Keywords |
Alanine/metabolism; Asparagine/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Diphosphates/metabolism; Diphosphonates/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Inorganic Pyrophosphatase/chemistry; Inorganic Pyrophosphatase/genetics; Inorganic Pyrophosphatase/metabolism; Magnesium/metabolism; Molecular Structure; Mutation; Protein Structure, Quaternary; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/metabolism |
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