PMID:9275296
| Citation |
Velichko, IS and Baykov, AA (1997) A hybrid mutant form of Escherichia coli inorganic pyrophosphatase. Biochemistry Mosc. 62:233-6 |
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| Abstract |
The inorganic pyrophosphatase of Escherichia coli is a tightly hexamer of identical subunits. Upon interaction of its two mutant forms in which the trimer-trimer contacts were weakened because of E20D and H136Q substitutions, a hybrid hexameric E20D/H136Q-PPase is formed. The catalytic activity of its constituent H136Q trimer is same of its hexamer, whereas metal-binding affinity is significantly decreased. These results point to an interdependence of two trimers in catalysis by hexameric pyrophosphatase. |
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| Keywords |
Binding Sites; Diphosphates/metabolism; Enzyme Activation; Escherichia coli/enzymology; Inorganic Pyrophosphatase; Kinetics; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Protein Multimerization; Pyrophosphatases/chemistry; Pyrophosphatases/genetics; Pyrophosphatases/metabolism |
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