Glycolate oxidase
From Proteopedia
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'''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>. | ||
| + | == Disease == | ||
| + | Mutations in GOX result in isolated asymptotic hyperoxaluria type I<ref>PMID:24996905</ref>. | ||
== Structural highlights == | == 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>. | 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>. | ||
Revision as of 09:32, 14 March 2016
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3D structures of glycolate oxidase
Updated on 14-March-2016
References
- ↑ 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
