Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis

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...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005-09, Vol.69 (9), p.1802-1805
Hauptverfasser:	Khan, M.I.H.(Shimane Univ., Matsue (Japan). Faculty of Life and Environmental Science), Kim, H, Ashida, H, Ishikawa, T, Shibata, H, Sawa, Y
Format:	Artikel
Sprache:	eng
Schlagworte:	BACILLUS SUBTILIS Bacillus subtilis - enzymology Bacillus subtilis - genetics Binding Sites - physiology Biological and medical sciences Fundamental and applied biological sciences. Psychology GLUTAMATE DEHYDROGENASE Glutamate Dehydrogenase - chemistry Glutamate Dehydrogenase - genetics Glutamate Dehydrogenase - physiology GLUTAMATE DESHYDROGENASE GLUTAMATO DESHIDROGENASA MICROBIAL PROPERTIES Models, Molecular MUTACION Mutagenesis, Site-Directed MUTATION PODER MICROBIANO PROPRIETE DES MICRO-ORGANISMES substrate specificity Substrate Specificity - genetics
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Zusammenfassung:	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 5.68s(-1), which were 265-fold and 473-fold higher respectively than those for 2-oxoglutarate.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.69.1802