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=' | |||
== 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>. | ||
Revision as of 12:16, 14 March 2016
<StructureSection load='2rdu' size='350' side='right' caption='Human α-defensin 1 (PDB entry 2pm4)' scene=>
FunctionFunction
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[1].
3D structures of glycolate oxidase3D structures of glycolate oxidase
Updated on 14-March-2016
ReferencesReferences
- ↑ Rojas CM, Senthil-Kumar M, Wang K, Ryu CM, Kaundal A, Mysore KS. Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis. Plant Cell. 2012 Jan;24(1):336-52. doi: 10.1105/tpc.111.093245. Epub 2012 Jan 27. PMID:22286136 doi:http://dx.doi.org/10.1105/tpc.111.093245