Structural highlights
Function
[GAOA_GIBZE] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Galactose oxidase (GO; EC 1.1.3.9) catalyses the oxidation of a wide range of primary alcohols including mono-, oligo- and polysaccharides. High-resolution structures have been determined for GO, but no structural information is available for the enzyme with bound substrate or inhibitor. Previously, computer-aided docking experiments have been used to develop a plausible model for interactions between GO and the D-galactose substrate. Residues implicated in such interactions include Arg330, Gln406, Phe464, Phe194 and Trp290. In the present study we describe an improved expression system for recombinant GO in the methylotrophic yeast Pichia pastoris. We use this system to express variant proteins mutated at Arg330 and Phe464 to explore the substrate binding model. We also demonstrate that the Arg330 variants display greater fructose oxidase activity than does wild-type GO.
Enhanced fructose oxidase activity in a galactose oxidase variant.,Deacon SE, Mahmoud K, Spooner RK, Firbank SJ, Knowles PF, Phillips SE, McPherson MJ Chembiochem. 2004 Jul 5;5(7):972-9. PMID:15239055[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Deacon SE, Mahmoud K, Spooner RK, Firbank SJ, Knowles PF, Phillips SE, McPherson MJ. Enhanced fructose oxidase activity in a galactose oxidase variant. Chembiochem. 2004 Jul 5;5(7):972-9. PMID:15239055 doi:10.1002/cbic.200300810
