Altering the Substrate Specificity of Glutamate Dehydrogenase from Bacillus subtilis by Site-Directed Mutagenesis

Md. Iqbal Hassan KHANDepartment of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University

Hyeung KIMDepartment of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University

Hiroyuki ASHIDADepartment of Molecular and Functional Genomics, Center for Integrated Research in Science, Shimane University

Takahiro ISHIKAWADepartment of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University

Hitoshi SHIBATADepartment of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University

Yoshihiro SAWADepartment of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University

Abstract

The Lys80, Gly82 and Met101 residues of glutamate dehydrogenase from Bacillus subtilis were mutated into a series of single mutants. The wild-type enzyme was highly specific for 2-oxoglutarate, whereas G82K and M101S dramatically switched to increased specificity for oxaloacetate with k _cat values 3.45 and 5.68 s⁻¹, which were 265-fold and 473-fold higher respectively than those for 2-oxoglutarate.

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Altering the Substrate Specificity of Glutamate Dehydrogenase from Bacillus subtilis by Site-Directed Mutagenesis

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Altering the Substrate Specificity of Glutamate Dehydrogenase from Bacillus subtilis by Site-Directed Mutagenesis

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