Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO3255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E.coli(Biochemistry & Molecular Biology)
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概要
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The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenases (GDHs) from E. coli, Gluconobacter oxydans, and Acinetobacter calcoaceticus except the N-terminal hydrophobic region of GDH. Additionally, the sldB gene located just upstream of sldA was found to encode a polypeptide consisting of 126 very hydrophobic residues that is similar in sequence to the one-sixth N-terminal region of the GDH. For the development of the SLDH activity in E. coli, co-expression of the sldA and sldB genes and the presence of pyrrloquinolone quinone as a co-factor were required.
- 2002-02-23
著者
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Hoshino Tatsuo
Departments of Medicine, Keio University and The Lankenau Hospital
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SHINJOH MASAKO
Department of Applied Microbiology, Nippon Roche Research Center
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Shinjoh M
Department Of Applied Microbiology Nippon Roche Research Center
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Shinjoh Masako
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino Tatsuo
Department Of Applied Microbiology Nippon Roche Research Center
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Miyazaki T
Department Of Applied Microbiology Nippon Roche Research Center
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TOMIYAMA Noribumi
Department of Applied Microbiology, Nippon Roche Research Center
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MIYAZAKI Taro
Department of Applied Microbiology, Nippon Roche Research Center
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Tomiyama Noribumi
Department Of Applied Microbiology Nippon Roche Research Center
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HOSHINO Tatsuo
Department of Applied Microbiology, Nippon Roche Research Center
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