Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 1997.07a
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- Pages.37-37
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- 1997
The Substrate Specificity of Pyranose Oxidase： the Activity of L-Gulono-1 4-lactone Oxidase
- Kwon, Jae-youl (Department of Microbiology, College of Natural Sciences and the Research Center for Molecular Microbiology, Seoul National University) ;
- Kang, Sa-Ouk (Department of Microbiology, College of Natural Sciences and the Research Center for Molecular Microbiology, Seoul National University)
- Published : 1997.07.01
Abstract
The catalytic efficiency of pyranose oxidase (EC 1.1.3.10.) determined for various sugars showed that D-glucose is the preferred substrate and the enzyme oxidized the various aldonolactones. The specificity constants of pyranose oxidase determined for deoxy- and deoxyfluoro-D-glucoses showed that a hydroxy group at C-4 of D-glucose acts as a hydrogen-bone acceptor, at C-6 as a hydrogen-bond donor, and at C-1 as a hydrogen-bond donor.(omitted)
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