Probing the Promiscuous Active Site of myo-Inositol Dehydrogenase Using Synthetic Substrates, Homology Modeling, and Active Site Modification

The active site of myo-inositol dehydrogenase (IDH, EC 1.1.1.18) from Bacillus subtilis recognizes a variety of mono- and disaccharides, as well as 1l-4-O-substituted inositol derivatives. It catalyzes the NAD+-dependent oxidation of the axial alcohol of these substrates with comparable kinetic cons...

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Veröffentlicht in:	Biochemistry (Easton) 2007-06, Vol.46 (25), p.7469-7477
Hauptverfasser:	Daniellou, Richard, Zheng, Hongyan, Langill, David M, Sanders, David A. R, Palmer, David R. J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus subtilis - enzymology Binding Sites Carbohydrate Conformation Catalysis Inositol - chemical synthesis Inositol - chemistry Inositol - genetics Kinetics Models, Molecular Molecular Sequence Data Molecular Structure Mutagenesis, Site-Directed Mutation Oxidation-Reduction Oxidoreductases - chemical synthesis Oxidoreductases - chemistry Oxidoreductases - genetics Protein Binding Sequence Homology, Amino Acid Structure-Activity Relationship Substrate Specificity
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