Pyranose oxidase identified as a member of the GMC oxidoreductase family
Author(s) -
Mario Albrecht,
Thomas Lengauer
Publication year - 2003
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btg140
Subject(s) - oxidoreductase , pyranose , biochemistry , homology (biology) , sequence alignment , biology , monosaccharide , enzyme , oxidase test , sequence homology , peptide sequence , genetics , amino acid , gene
Fungal pyranose oxidase is a flavoenzyme whose preferred substrate among several monosaccharides is D-glucose. After a comprehensive analysis of conserved features in a structure-based multiple sequence alignment of homologous proteins, we could classify this enzyme into the GMC oxidoreductase family. The identified homology also suggests a three-dimensional protein structure similar to the functionally related glucose oxidase.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom