Article
Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH.
The Journal of biological chemistry - 13 Nov 2009
Pennacchietti Eugenia, Lammens Tijs M, Capitani Guido, Franssen Maurice C R, John Robert A, Bossa Francesco, De Biase Daniela
Abstract excerpt
Glutamate decarboxylase (GadB) from Escherichia coli is a hexameric, pyridoxal 5'-phosphate-dependent enzyme catalyzing CO(2) release from the alpha-carboxyl group of L-glutamate to yield gamma-aminobutyrate. GadB exhibits an acidic pH optimum and undergoes a spectroscopically detectable and strongly cooperative pH-dependent conformational change involving at least six protons. Crystallographic studies showed...
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