Glycolate oxidase: Difference between revisions

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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/2'>homotetramer</scene>. GOX structure shows the <scene name='48/486364/Cv/3'>typical β8/α8 fold</scene> of an α-hydroxy acid oxidase and its <scene name='48/486364/Cv/6'>active site contains the cofactor FMN</scene><ref>PMID:18215067</ref>.  
The biological assembly of human glycolate oxidase 1 <scene name='48/486364/Cv/2'>homotetramer</scene>. GOX structure shows the <scene name='48/486364/Cv/3'>typical β8/α8 fold</scene> ({{Template:ColorKey_Helix}},
{{Template:ColorKey_Strand}},
{{Template:ColorKey_Loop}},
{{Template:ColorKey_Turn}}
) of an α-hydroxy acid oxidase and its <scene name='48/486364/Cv/6'>active site contains the cofactor FMN</scene><ref>PMID:18215067</ref>. Water molecules shown as red spheres.  
</StructureSection>
</StructureSection>
==3D structures of glycolate oxidase==
==3D structures of glycolate oxidase==

Revision as of 12:19, 20 March 2016

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[1].

Disease

Mutations in GOX result in isolated asymptotic hyperoxaluria type I[2].

Structural highlights

The 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 shown as red spheres.

Human glycolate oxidase 1 complex with glyoxylate and FMN (PDB entry 2rdu)

Drag the structure with the mouse to rotate

3D structures of glycolate oxidase3D structures of glycolate oxidase

Updated on 20-March-2016

ReferencesReferences

  1. 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
  2. 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
  3. 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

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