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PDBsum entry 2jkx
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Oxidoreductase
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PDB id
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2jkx
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Galactose oxidase. Matgo. Copper free, expressed in pichia pastoris.
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Structure:
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Galactose oxidase. Chain: a. Fragment: residues 42-680. Synonym: gao, goase, go. Engineered: yes. Other_details: thioether bond between cys228 and tyr272
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Source:
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Gibberella zeae. Organism_taxid: 5518. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
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Resolution:
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1.84Å
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R-factor:
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0.167
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R-free:
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0.201
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Authors:
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S.E.Deacon,K.Mahmoud,R.K.Spooner,S.J.Firbank,P.F.Knowles, S.E.V.Phillips,M.J.Mcpherson
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Key ref:
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S.E.Deacon
et al.
(2004).
Enhanced fructose oxidase activity in a galactose oxidase variant.
Chembiochem,
5,
972-979.
PubMed id:
DOI:
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Date:
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01-Sep-08
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Release date:
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09-Sep-08
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PROCHECK
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Headers
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References
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P0CS93
(GAOA_GIBZA) -
Galactose oxidase from Gibberella zeae
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Seq:
Struc:
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680 a.a.
639 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.1.1.3.9
- galactose oxidase.
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Reaction:
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D-galactose + O2 = D-galacto-hexodialdose + H2O2
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D-galactose
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+
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O2
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=
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D-galacto-hexodialdose
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+
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H2O2
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Cofactor:
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Cu cation
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Chembiochem
5:972-979
(2004)
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PubMed id:
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Enhanced fructose oxidase activity in a galactose oxidase variant.
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S.E.Deacon,
K.Mahmoud,
R.K.Spooner,
S.J.Firbank,
P.F.Knowles,
S.E.Phillips,
M.J.McPherson.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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O.Spadiut,
L.Olsson,
and
H.Brumer
(2010).
A comparative summary of expression systems for the recombinant production of galactose oxidase.
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Microb Cell Fact,
9,
68.
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F.Escalettes,
and
N.J.Turner
(2008).
Directed evolution of galactose oxidase: generation of enantioselective secondary alcohol oxidases.
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Chembiochem,
9,
857-860.
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M.S.Rogers,
R.Hurtado-Guerrero,
S.J.Firbank,
M.A.Halcrow,
D.M.Dooley,
S.E.Phillips,
P.F.Knowles,
and
M.J.McPherson
(2008).
Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.
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Biochemistry,
47,
10428-10439.
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PDB codes:
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M.S.Rogers,
E.M.Tyler,
N.Akyumani,
C.R.Kurtis,
R.K.Spooner,
S.E.Deacon,
S.Tamber,
S.J.Firbank,
K.Mahmoud,
P.F.Knowles,
S.E.Phillips,
M.J.McPherson,
and
D.M.Dooley
(2007).
The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis.
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Biochemistry,
46,
4606-4618.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
