Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase

The double-site variant (C450S-N475K) L-arabinose isomerase (L-AI) from Geobacillus thermodenitrificans catalyzes the isomerization of D-galactose to D-tagatose, a functional sweetener. Using a substrate-docking homology model, the residues near to D-galactose O6 were identified as Met186, Phe280, a...

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Veröffentlicht in:	Applied microbiology and biotechnology 2014-11, Vol.98 (22), p.9271-9281
Hauptverfasser:	Kim, Baek-Joong, Hong, Seung-Hye, Shin, Kyung-Chul, Jo, Ye-Seul, Oh, Deok-Kun
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldose-Ketose Isomerases - genetics Aldose-Ketose Isomerases - metabolism Amino Acid Substitution Amino acids Arabinose - metabolism Bacillus thermodenitrificans Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology catalytic activity Cloning Crystal structure E coli Energy Enzymes Galactose - metabolism Geobacillus Geobacillus - enzymology Geobacillus - genetics Gram-positive bacteria Hexoses - metabolism Isomerases isomerization Kinetics Life Sciences Microbial Genetics and Genomics Microbiology Mutagenesis Mutagenesis, Site-Directed Mutant Proteins - genetics Mutant Proteins - metabolism Mutation Mutation, Missense Physiological aspects Properties Proteins site-directed mutagenesis Studies Substrate Specificity
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