 |
PDBsum entry 2jkx
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
2jkx
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Enhanced fructose oxidase activity in a galactose oxidase variant.
|
|
|
Authors
|
|
S.E.Deacon,
K.Mahmoud,
R.K.Spooner,
S.J.Firbank,
P.F.Knowles,
S.E.Phillips,
M.J.Mcpherson.
|
|
|
Ref.
|
|
Chembiochem, 2004,
5,
972-979.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
