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Literature summary for 1.1.3.15 extracted from
- Plant and animal glycolate oxidases have a common eukaryotic ancestor and convergently duplicated to evolve long-chain 2-hydroxy acid oxidases (2014), Mol. Biol. Evol., 31, 1089-1101 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genes Glo1, sequence comparisons, phylogenetic analysis and tree | Arabidopsis thaliana |
| genes Glo3, sequence comparisons, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR (DE3) pLysS | Arabidopsis thaliana |
| genes Glo4, sequence comparisons, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR DE3 pLysS | Arabidopsis thaliana |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| peroxisome | - |
Arabidopsis thaliana | 5777 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-hydroxycaproate + O2 | Arabidopsis thaliana | - |
2-oxocaproate + H2O2 | - |
? |  |
| 2-hydroxycaprylate + O2 | Arabidopsis thaliana | - |
2-oxocaprylate + H2O2 | - |
? | |
| 2-hydroxypalmitate + O2 | Arabidopsis thaliana | - |
2-oxopalmitate + H2O2 | - |
? | |
| an (S)-2-hydroxy carboxylate + O2 | Arabidopsis thaliana | - |
a 2-oxo carboxylate + H2O2 | - |
? | |
| L-lactate + O2 | Arabidopsis thaliana | - |
pyruvate + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | Q24JJ8 | - |
- |
| Arabidopsis thaliana | Q9LJH5 | - |
- |
| Arabidopsis thaliana | Q9LRR9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BLR DE3 pLysS by nickel affinity chromatography and desalting gel filtration to homogeneity | Arabidopsis thaliana |
| recombinant His-tagged enzyme from Escherichia coli strain BLR(DE3) pLysS by nickel affinity chromatography and desalting gel filtration to homogeneity | Arabidopsis thaliana |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-hydroxycaproate + O2 | - |
Arabidopsis thaliana | 2-oxocaproate + H2O2 | - |
? | |
| 2-hydroxycaprylate + O2 | - |
Arabidopsis thaliana | 2-oxocaprylate + H2O2 | - |
? | |
| 2-hydroxydodecanoate + O2 | - |
Arabidopsis thaliana | 2-oxododecanoate + H2O2 | - |
? | |
| 2-hydroxyisocaproate + O2 | - |
Arabidopsis thaliana | 2-oxoisocaproate + H2O2 | - |
? | |
| 2-hydroxypalmitate + O2 | - |
Arabidopsis thaliana | 2-oxopalmitate + H2O2 | - |
? | |
| an (S)-2-hydroxy carboxylate + O2 | - |
Arabidopsis thaliana | a 2-oxo carboxylate + H2O2 | - |
? | |
| isoleucic acid + O2 | - |
Arabidopsis thaliana | ? + H2O2 | - |
? | |
| L-lactate + O2 | - |
Arabidopsis thaliana | pyruvate + H2O2 | - |
? | |
| additional information | isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate | Arabidopsis thaliana | ? | - |
? | |
| additional information | isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate | Arabidopsis thaliana | ? | - |
? | |
| valic acid + O2 | - |
Arabidopsis thaliana | ? + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 39900, recombinant enzyme without tag, SDS-PAGE | Arabidopsis thaliana |
| ? | x * 40100, recombinant enzyme without tag, SDS-PAGE | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (L)-2-HAOX | - |
Arabidopsis thaliana |
| Glo1 | - |
Arabidopsis thaliana |
| GLO3 | - |
Arabidopsis thaliana |
| Glo4 | - |
Arabidopsis thaliana |
| glycolate oxidase | - |
Arabidopsis thaliana |
| GOX1 | - |
Arabidopsis thaliana |
| lHAOX1 | - |
Arabidopsis thaliana |
| lHAOX2 | - |
Arabidopsis thaliana |
| long-chain 2-hydroxy acid oxidase | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Arabidopsis thaliana |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
assay at | Arabidopsis thaliana |
| 7.5 | - |
assay at | Arabidopsis thaliana |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Arabidopsis thaliana |
| 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 | Arabidopsis thaliana |
| additional information | structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX | Arabidopsis thaliana |
| additional information | structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX | Arabidopsis thaliana |
| additional information | structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX | Arabidopsis thaliana |
| physiological function | glycolate oxidase (GOX) is a crucial enzyme of plant photorespiration | Arabidopsis thaliana |
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Release 2023.1 (January 2023)
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