Glycolate oxidase: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='350' side='right' caption='Human glycolate oxidase 1 complex with glyoxylate and FMN (PDB entry [[2rdu]])' scene='48/486364/Cv/1'> | ||
== 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) or '''hydroxyacid oxidase''' 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>. | ||
== Disease == | == Disease == | ||
Mutations in GOX result in isolated asymptotic hyperoxaluria type I<ref>PMID:24996905</ref>. | Mutations in GOX result in isolated asymptotic hyperoxaluria type I<ref>PMID:24996905</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
The biological assembly of human glycolate oxidase 1 <scene name='48/486364/Cv/ | The biological assembly of human glycolate oxidase 1 <scene name='48/486364/Cv/7'>homotetramer</scene>. GOX structure shows the <scene name='48/486364/Cv/8'>typical β8/α8 fold</scene> ({{Template:ColorKey_Helix}}, | ||
{{Template:ColorKey_Strand}}, | {{Template:ColorKey_Strand}}, | ||
{{Template:ColorKey_Loop}}, | {{Template:ColorKey_Loop}}, | ||
{{Template:ColorKey_Turn}} | {{Template:ColorKey_Turn}} | ||
) of an α-hydroxy acid oxidase and its <scene name='48/486364/Cv/ | ) of an α-hydroxy acid oxidase and its <scene name='48/486364/Cv/9'>active site contains the cofactor FMN</scene><ref>PMID:18215067</ref>. Water molecules are shown as red spheres. | ||
==3D structures of glycolate oxidase== | ==3D structures of glycolate oxidase== | ||
[[Glycolate oxidase 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 12:52, 6 August 2020
FunctionGlycolate oxidase (GOX) or hydroxyacid oxidase 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]. DiseaseMutations in GOX result in isolated asymptotic hyperoxaluria type I[2]. Structural highlightsThe biological assembly of human glycolate oxidase 1 . GOX structure shows the (Alpha Helices, Beta Strands , Loops , Turns ) of an α-hydroxy acid oxidase and its [3]. Water molecules are shown as red spheres. 3D structures of glycolate oxidaseGlycolate oxidase 3D structures
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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
- ↑ Frishberg Y, Zeharia A, Lyakhovetsky R, Bargal R, Belostotsky R. Mutations in HAO1 encoding glycolate oxidase cause isolated glycolic aciduria. J Med Genet. 2014 Aug;51(8):526-9. doi: 10.1136/jmedgenet-2014-102529. Epub 2014 , Jul 4. PMID:24996905 doi:http://dx.doi.org/10.1136/jmedgenet-2014-102529
- ↑ Murray MS, Holmes RP, Lowther WT. Active Site and Loop 4 Movements within Human Glycolate Oxidase: Implications for Substrate Specificity and Drug Design. Biochemistry. 2008 Feb 26;47(8):2439-49. Epub 2008 Jan 24. PMID:18215067 doi:10.1021/bi701710r