The Tetramer Structure of the Glycoside Hydrolase Family 27 α-Galactosidase I from Umbelopsis vinacea
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概要
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The crystal structure of Umbelopsis vinacea α-galactosidase I, which belongs to glycoside hydrolase family 27, was determined at 2.0 Å resolution. The monomer structure was well conserved with those of glycoside hydrolase family 27 enzymes. The biological tetramer structure of this enzyme was constructed by the crystallographic 4-fold symmetry, and tetramerization appeared to be caused by three inserted peptides that were involved in the tetramer interface. The quaternary structure indicated that the substrate specificity of this enzyme might be related to the tetramer formation. Three N-glycosylated sugar chains were observed, and their structures were found to be of the high-mannose type.
- 社団法人 日本農芸化学会の論文
- 2009-10-23
著者
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Kim Wook-Dong
Food Biotechnology Division, National Food Research Institute
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PARK Gwi-Gun
Food Biotechnology Division, National Food Research Institute
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KOBAYASHI Hideyuki
Food Biotechnology Division, National Food Research Institute
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Kaneko Satoshi
Food Biotechnology Div. National Food Res. Inst.
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Fujimoto Zui
Protein Research Unit National Institute Of Agrobiological Sciences
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Kaneko Satoshi
Food Biotechnology Division National Food Research Institute
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Kin Wook-dong
Food Biotechnology Division National Food Research Institute
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Park Gwi-gun
Food Biotechnology Division National Food Research Institute
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Momma Mitsuru
Protein Research Unit National Institute Of Agrobiological Sciences
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Kim Wook-dong
Food Biotechnology Division National Food Research Institute National Agriculture And Food Research
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Kobayashi Hideyuki
Food Biotechnology Division National Food Research Institute
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