Glycolate oxidase: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 11: | Line 11: | ||
{{Template:ColorKey_Turn}} | {{Template:ColorKey_Turn}} | ||
) 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. | ) 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== | |||
[[Glycolate oxidase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
==3D structures of glycolate oxidase== | ==3D structures of glycolate oxidase== | ||
| Line 19: | Line 23: | ||
*Glycolate oxidase | *Glycolate oxidase | ||
**[[1gyl]] – sGOX – spinach<br /> | **[[1tb3]] – rGOX3 + FMN – rat<br /> | ||
**[[ | **[[1gyl]], [[1gox]] – sGOX + FMN – spinach<br /> | ||
**[[5zbn]] – NbGOX – ''Nicotiana benthamiana''<br /> | |||
**[[5zbm]] – NbGOX + FMN <br /> | |||
**[[2yvs]] – GOX GLCE subunit – ''Thermus thermophilus''<br /> | **[[2yvs]] – GOX GLCE subunit – ''Thermus thermophilus''<br /> | ||
*Glycolate oxidase complex | *Glycolate oxidase complex | ||
**[[ | **[[2rdu]], [[2nzl]] – hGOX1 + FMN + glyoxylate<br /> | ||
**[[ | **[[2rdw]] – hGOX1 + FMN + sulfate<br /> | ||
**[[ | **[[6gmb]] – hGOX1 + FMN + glycolate<br /> | ||
**[[2w0u]], [[2rdt]] – hGOX1 + | **[[6gmc]], [[2w0u]], [[2rdt]] – hGOX1 + FMN + thiadiazole derivative<br /> | ||
**[[3sgz]] – rGOX2 + | **[[5qib]], [[5qid]], [[6qif]] – hGOX1 + FMN + pyrimidine derivative<br /> | ||
**[[5qic]] – hGOX1 + FMN + piperazine derivative<br /> | |||
**[[5qie]] – hGOX1 + FMN + aniline derivative<br /> | |||
**[[6qig]], [[6qih]] – hGOX1 + FMN + imidazole derivative<br /> | |||
**[[3sgz]] – rGOX2 + FMN + thiadiazole derivative<br /> | |||
**[[1al8]], [[1al7]] – sGOX + FMN + thiadiazole derivative<br /> | |||
**[[3giy]] – GOX1/(S)-mandelate dehydrogenase + MES – ''Pseudomonas putida'' | **[[3giy]] – GOX1/(S)-mandelate dehydrogenase + MES – ''Pseudomonas putida'' | ||
}} | }} | ||
Revision as of 12:51, 15 July 2019
FunctionGlycolate 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]. 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
|
| ||||||||||
3D structures of glycolate oxidase3D structures of glycolate oxidase
Updated on 15-July-2019
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