Site directed mutagenesis studies of FAD-dependent glucose dehydrogenase catalytic subunit of Burkholderia cepacia

• Published in: Biotechnology letters Vol. 30; no. 11; pp. 1967 - 1972
• Main Authors: Yamaoka, Hideaki, Yamashita, Yuki, Ferri, Stefano, Sode, Koji
• Format: Journal Article
• Language: English
• Published: Dordrecht Dordrecht : Springer Netherlands 01.11.2008; Springer Netherlands; Springer; Springer Nature B.V
• Subjects: Alanine - genetics; Amino Acid Sequence; Applied Microbiology; Asparagine - genetics; Base Sequence; Biochemistry; Biological and medical sciences; Biomedical and Life Sciences; Biotechnology; Burkholderia cepacia; Burkholderia cepacia - enzymology; Burkholderia cepacia - genetics; Burkholderia cepacia - metabolism; Catalytic Domain - genetics; Dehydrogenase; Diabetes; Enzymes; Flavin-Adenine Dinucleotide - metabolism; Fundamental and applied biological sciences. Psychology; Glucose; Glucose - metabolism; Glucose 1-Dehydrogenase - genetics; Glucose 1-Dehydrogenase - metabolism; Life Sciences; Microbiology; Molecular Sequence Data; Mutagenesis, Site-Directed - methods; Mutation; Original Research Paper; Sequence Homology, Amino Acid; Substrate Specificity; Substrates; Glucose dehydrogenase; Glucose sensor; Diabetes; Substrate specificity; Enzyme; Diabetes mellitus; Site directed mutagenesis; Glucose 1-dehydrogenase; Subunit; Detector; Burkholderia cepacia; Bacteria; Oxidoreductases

A FAD-dependent glucose dehydrogenase (FADGDH) mutant with narrow substrate specificity was constructed by site-directed mutagenesis. Several characteristics of FADGDH, such as high catalytic activity and high electron transfer ability, make this enzyme suitable for application to glucose sensors. H...