Glycolate oxidase: Difference between revisions

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{{STRUCTURE_2w0u|  PDB=2w0u | SIZE=400| SCENE= |right|CAPTION=Human glycolate oxidase 1 complex with glyoxylate, [[2w0u]] }}
{{STRUCTURE_1gyl|  PDB=1gyl | SIZE=400| SCENE= |right|CAPTION=Human glycolate oxidase 1 complex with glyoxylate, [[1gyl]] }}
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Revision as of 11:41, 4 November 2012

Template:STRUCTURE 1gyl Glycolate oxidase (GOX) catalyzes the conversion of (S)-2-hydroxy acid and molecular oxygen to 2-oxo acid and hydrogen peroxide. In higher plants, GOX catalyzes the oxidation of glycolate to glyoxylate. GOX is part of the glyoxylate and dicarboxylate metabolism and uses FMN as a cofactor. GOX catalyzes the first step in the utilization of glycolate as the sole source of carbon.

3D structures of glycolate oxidase3D structures of glycolate oxidase

1gyl – sGOX – spinach
2nzl – hGOX1 – human
2yvs – GOX GLCE subunit – Thermus thermophilus
1tb3 – rGOX3 – rat

Glycolate oxidase complex

1al8, 1al7 – sGOX + inhibitor
2rdu – hGOX1 + glyoxylate
2rdw – hGOX1 + sulfate
2w0u, 2rdt – hGOX1 + inhibitor
3sgz – rGOX2 + inhibitor
3giy – GOX1/(S)-mandelate dehydrogenase + MES – Pseudomonas putida

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman