The Tetramer Structure of the Glycoside Hydrolase Family 27 α-Galactosidase I fromUmbelopsis vinacea | Zendy

Zui Fujimoto | Zendy; Satoshi Kaneko | Zendy; Wook-Dong Kim | Zendy; Gwi-Gun Park | Zendy; Mitsuru Momma | Zendy; Hideyuki Kobayashi | Zendy

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The Tetramer Structure of the Glycoside Hydrolase Family 27 α-Galactosidase I fromUmbelopsis vinacea

Author(s) -

Zui Fujimoto,

Satoshi Kaneko,

Wook-Dong Kim,

Gwi-Gun Park,

Mitsuru Momma,

Hideyuki Kobayashi

Publication year - 2009

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.90604

Subject(s) - tetramer , hydrolase , glycoside hydrolase , protein quaternary structure , chemistry , stereochemistry , enzyme , monomer , biochemistry , crystallography , organic chemistry , protein subunit , gene , polymer

The crystal structure of Umbelopsis vinacea alpha-galactosidase I, which belongs to glycoside hydrolase family 27, was determined at 2.0 A 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.

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