Glycolate oxidase: Difference between revisions

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<StructureSection load='2rdu' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
<StructureSection load='2rdu' size='350' side='right' caption='Human glycolate oxidase 1 complex with glyoxylte (PDB entry [[2rdu]])' scene=''>
== Function ==
== Function ==
'''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<ref>PMID:22286136</ref>.   
'''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<ref>PMID:22286136</ref>.   


== Structural highlights ==
GOX structure shows the typical β8/α8 fold of an α-hydroxy acid oxidase and its active site contains the cofactor FMN<ref>PMID:18215067</ref>.
</StructureSection>
==3D structures of glycolate oxidase==
==3D structures of glycolate oxidase==


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Michal Harel, Alexander Berchansky, Joel L. Sussman