2JKX

Galactose oxidase. MatGO. Copper free, expressed in Pichia Pastoris.

Summary for 2JKX

• Entry DOI: 10.2210/pdb2jkx/pdb
• Related: 1GOF 1GOG 1GOH 1K3I 1T2X 2VZ1 2VZ3
• Descriptor: GALACTOSE OXIDASE, ACETATE ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: metal-binding, thioether bond, oxidoreductase, copper, secreted, oxidases, kelch repeat, copper enzymes, enzyme catalysis, protein engineering
• Biological source: GIBBERELLA ZEAE
• Total number of polymer chains: 1
• Total formula weight: 68677.72

Authors

Deacon, S.E.,Mahmoud, K.,Spooner, R.K.,Firbank, S.J.,Knowles, P.F.,Phillips, S.E.V.,McPherson, M.J. (deposition date: 2008-09-01, release date: 2008-09-09, Last modification date: 2024-11-20)

Primary citation

Deacon, S.E.,Mahmoud, K.,Spooner, R.K.,Firbank, S.J.,Knowles, P.F.,Phillips, S.E.V.,McPherson, M.J.
Enhanced Fructose Oxidase Activity in a Galactose Oxidase Variant
Chembiochem, 5:972-, 2004

PubMed 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.

PubMed: 15239055
DOI: 10.1002/CBIC.200300810

Experimental method

X-RAY DIFFRACTION (1.84 Å)