EC Number   |
General Information |
Reference |
|---|
    1.1.3.15 | evolution |
enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. Vertebrates possess lHAOX proteins acting on similar substrates as plant lHAOX. The existence of GOX and lHAOX subfamilies in both plants and animals is not due to shared ancestry but is the result of convergent evolution in the two most complex eukaryotic lineages. Duplication and diversification occurred independently at the base of deuterostomia and at the base of vascular plants. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview. Convergent evolution in vascular plants and deuterostomia |
745737 |
| 1.1.3.15 | evolution |
enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). The encoding gene is thought to have originated from endosymbiotic gene transfer between the eukaryotic host and the cyanobacterial endosymbiont at the base of plantae. Animals also possess GOX activities. Plant and animal GOX belong to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview |
745737 |
| 1.1.3.15 | evolution |
the enzyme belongs to the family of L-2-hydroxy acid oxidases |
-, 745481, 745609 |
| 1.1.3.15 | evolution |
the enzyme is a member of the flavoenzyme family |
724535 |
| 1.1.3.15 | malfunction |
an alternative approach to prevent glyoxylate production in subjects with primary hyperoxaluria type 1 (PH1) is using Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, which encodes glycolate oxidase (GO), to reduce the hepatic conversion of glycolate to glyoxylate. This approach efficiently reduces GO mRNA and protein in the livers of mice. Reduction of hepatic GO leads to normalization of urine oxalate levels and reduces CaOx deposition in a preclinical mouse model of PH1. Hao1-/- mice show elevated levels of urinary glycolate without renal damage or other phenotypic consequences |
-, 745815 |
| 1.1.3.15 | malfunction |
evaluation of the potential of siRNAs targeting the synthesis of liver glycolate oxidase or hydroxyproline dehydrogenase formulated in lipid nanoparticles, to reduce urinary oxalate excretion in Agxt KO mice. The siRNA targeting glycolate oxidase blocks a downstream step and prevents the synthesis of glyoxylate from glycolate in the liver. The ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans |
-, 741999 |
| 1.1.3.15 | malfunction |
the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones |
698951 |
| 1.1.3.15 | metabolism |
inactivation of gene pox encoding pyruvate oxidase causes a dramatic reduction in H2O2 production from lactate, suggesting a synergistic action of the two oxidases in converting lactate into H2O2. The pox mutant of Streptomyces oligofermentans fails to inhibit Streptomyces mutans even though lox is active |
724014 |
| 1.1.3.15 | metabolism |
the enzyme is involved in the glyoxylate metabolism, overview |
700815 |
| 1.1.3.15 | metabolism |
the enzyme is involved in the metabolism of glycolate |
701203 |
