PDBsum entry: 2f6c

Oxidoreductase

PDB id: 2f6c

Contents

Protein chain

577 a.a. *

Ligands

FAD

PG4

PEG

Waters ×595

* Residue conservation analysis

PDB id:

2f6c

Name:

Oxidoreductase

Title:

Reaction geometry and thermostability of pyranose 2-oxidase white-rot fungus peniophora sp., Thermostability mutant e54

Structure:

Pyranose 2-oxidase. Chain: a. Synonym: p2ox, pyranose oxidase, prod, pod, pox, pyranose:o oxidoreductase, glucose 2-oxidase, fad-oxidoreductase. Engineered: yes. Mutation: yes

Source:

Peniophora sp. Sg. Organism_taxid: 204723. Gene: p2ox, poxsg. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Tetramer (from PDB file)

Resolution:

1.84Å R-factor: 0.152 R-free: 0.186

Authors:

M.Bannwarth,D.M.Heckmann-Pohl,S.Bastian,F.Giffhorn,G.E.Schul

Key ref:

M.Bannwarth et al. (2006). Reaction geometry and thermostable variant of pyranose 2-oxidase from the white-rot fungus Peniophora sp. Biochemistry, 45, 6587-6595. PubMed id: 16716069 DOI: 10.1021/bi052465d

Date:

29-Nov-05 Release date: 13-Jun-06

Protein chain

Q8J136  (P2OX_PENSG) -  Pyranose 2-oxidase

Seq: 623 a.a.

Struc: 577 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.1.1.3.10 - Pyranose oxidase.
• Reaction: D-glucose + O₂ = 2-dehydro-D-glucose + H₂O₂

D-glucose (Bound ligand (Het Group name = PEG) matches with 58.33% similarity) + O(2) = 2-dehydro-D-glucose + H(2)O(2)

• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: periplasmic space (1 term)
• Biological process: oxidation-reduction process (2 terms)
• Biochemical function: oxidoreductase activity (4 terms)

reference

DOI no: 10.1021/bi052465d

Biochemistry 45:6587-6595 (2006)

PubMed id: 16716069

Reaction geometry and thermostable variant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.

M.Bannwarth, D.Heckmann-Pohl, S.Bastian, F.Giffhorn, G.E.Schulz.

ABSTRACT

Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates using dioxygen; glucose, for example, is oxidized at carbon 2. The structure of pyranose 2-oxidase with the reaction product 2-keto-beta-d-glucose bound in the active center is reported in a new crystal form at 1.41 A resolution. The binding structure suggests that the alpha-anomer cannot be processed. The binding mode of the oxidized product was used to model other sugars accepted by the enzyme and to explain its specificity and catalytic rates. The reported structure at pH 6.0 shows a drastic conformational change in the loop of residues 454-461 (loop 454-461) at the active center compared to that of a closely homologous enzyme analyzed at pH 4.5 with a bound acetate inhibitor. In our structures, the loop is highly mobile and shifts to make way for the sugar to pass into the active center. Presumably, loop 454-461 functions as a gatekeeper. Apart from the wild-type enzyme, a thermostable variant was analyzed at 1.84 A resolution. In this variant, Glu542 is exchanged for a lysine. The observed stabilization could be a result of the mutated residue changing an ionic contact at a comparatively weak interface of the tetramer.