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evolution
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the enzyme is a member of the flavoenzyme family
evolution
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the enzyme is a member of the flavoenzyme family
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
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
evolution
the enzyme belongs to the family of L-2-hydroxy acid oxidases
evolution
the enzyme belongs to the family of L-2-hydroxy acid oxidases
evolution
the enzyme belongs to the family of L-2-hydroxy acid oxidases
evolution
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the enzyme belongs to the family of L-2-hydroxy acid oxidases
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evolution
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the enzyme belongs to the family of L-2-hydroxy acid oxidases
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malfunction
the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
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
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
malfunction
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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
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malfunction
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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
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metabolism
the enzyme is involved in the glyoxylate metabolism, overview
metabolism
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the enzyme is involved in the metabolism of glycolate
metabolism
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the enzyme is involved in the metabolism of glycolate, glycolate oxidase is a key enzyme involved in C3 photorespiration metabolic pathway, the process where plants lose up to half of assimilated carbon
metabolism
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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
physiological function
a positive and linear correlation exists between GLO activities and the net photosynthetic rates, PN, and photoinhibition subsequently occurrs once PN reduction surpasses 60%, indicating GLO can exert a strong regulation over photosynthesis. Isocitrate lyase and malate synthase, two key enzymes in the glyoxylate cycle, are highly up-regulated under GLO deficiency
physiological function
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role in C3 and C4 plants and associated regulation mechanisms
physiological function
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role in C3 and C4 plants and associated regulation mechanisms
physiological function
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the enzyme performs an essential step in the operation of the oxidative photorespiratory cycle accompanying photosynthetic CO2 assimilation in C3 plants
physiological function
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H2O2 production, especially lactate oxidase, allows Streptomyces oligofermentans to out-compete Streptomyces mutans in oral commensals, the enzyme mainly contributes to H2O2 production in stationary phase. But lactate oxidase requires cofunction of pyruvate oxidase for successfully inhibiting Streptomyces mutans
physiological function
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pharmacological role of the enzyme in the management of blood pressure
physiological function
glycolate oxidase (GOX) is a crucial enzyme of plant photorespiration
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
barley stripe mosaic virus BSMV gammab protein inhibits GOX enzymatic activity, peroxisomal free radicals, and ROS bursts under BSMV infection. GOX interacts with virus protein BSMV gammab. Deletion of gammab from BSMV abolishes inhibition of GOX activity in vivo, and GOX enzymatic activity is reduced in gammab transiently expressing cells. Presence of a GST-gammab construct greatly reduces recombinant GOX enzymatic activity. GOX mRNA decreases during BSMV infection
physiological function
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inoculation of plants with Pseudomonas syringae increases photorespiration rate and expression of glycolate oxidase (GOX2), serine glyoxylate aminotransferase (SGT) and serine hydroxyl methyltransferase (SHMT1). Silencing of GOX2, SGT or SHMT1 genes in tomato decreases photorespiration but increases susceptibility to Pseudomonas syringae, whereas transient overexpression of GOX2, SGT or SHMT1 in tobacco increases basal defence. Salicylic acid signalling is involved in GOX2-mediated, SGT-mediated and SHMT1-mediated defence. H2O2 pretreatment remarkably alleviates the GOX2 silencing-induced depression in basal defence and salicylic acid signalling
physiological function
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sixteen GOX genes are found in Nicotiana benthamiana genome. They consist of GOX and HAOX groups. All but two GOX proteins contain an alpha_hydroxyacid_oxid_FMN domain with extra 433-52 amino acids compared to that of FMN-dependent alpha-hydroxyacid oxidizing enzymes. Silencing of three GOX family genes NbHAOX8, NbGOX1 and NbGOX4 differently affects resistance to various pathogens including Tobacco rattle virus, Xanthomonas oryzae pv. oryzae (Xoo) and Sclerotinia sclerotiorum. Effect of these genes on resistance to Xoo is well correlated with that on Xoo-responsive H2O2 accumulation. Silencing of these genes enhances PAMP peptide flg22-triggered immunity
physiological function
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L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
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physiological function
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L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
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additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
the key residue Tyr129 in the active site of LCHAO does affect L-lactate binding to LCHAO but plays an important role on the catalytic reaction process through an H-bond interaction. Generation of a structural model of LCHAO-FMN-lactate. The active site informed by residues Phe23, Tyr129, Asp157, Arg164, Lys223, His247, and Arg250