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Literature summary extracted from

  • Pennati, A.; Gadda, G.
    Involvement of ionizable groups in catalysis of human liver glycolate oxidase (2009), J. Biol. Chem., 284, 31214-31222.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.1.3.15 drug development in humans the enzyme is a potential drug target for treatment of primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.15 H260A site-directed mutagenesis Homo sapiens
1.1.3.15 H260Q site-directed mutagenesis Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.15 chloride inhibits the enzyme at high concentrations Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.15 additional information
-
additional information stopped-flow, steady-state, and presteady-state kinetics at different pH values, pH profiles, detailed overview Homo sapiens
1.1.3.15 0.2
-
glycolate pH 7.5, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 0.23
-
glycolate pH 7.0, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 0.44
-
O2 pH 7.5, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 0.59
-
O2 pH 9.0, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 0.64
-
O2 pH 7.0, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 2
-
glycolate pH 9.0, 30°C, recombinant enzyme, first order Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.15 peroxisome
-
Homo sapiens 5777
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.15 glycolate + O2 Homo sapiens
-
glyoxylate + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.15 Homo sapiens Q9UJM8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.15 recombinant enzyme by nickel affinity chromatography, ammonium sulfate fractionation and dialysis Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.15 an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2 the pH affects the kinetic steps of the catalytic mechanism of human glycolate oxidase, the enzyme shows a ping-pong bi-bi kinetic mechanism between pH 6.0 and 10.0, overview. Formation of the enzyme-substrate complex suggests the presence of a protonated group participating in substrate binding Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.15 liver
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.15 glycolate + O2
-
Homo sapiens glyoxylate + H2O2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.15 glycolate oxidase
-
Homo sapiens
1.1.3.15 GOX
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.15 30
-
assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.15 additional information
-
additional information a second-order rate constant for the capture of glycolate (kcat/Kglycolate) of 68300 M/s, and a second-order rate constant for reaction of the reduced flavin with oxygen (kcat/Koxygen) of 24500 Ms Homo sapiens
1.1.3.15 15.7
-
glycolate pH 7.0, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 20
-
glycolate pH 7.5, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 31.2
-
glycolate pH 9.0, 30°C, recombinant enzyme, first order Homo sapiens
1.1.3.15 54.1
-
flavin pH 7.0, 30°C, flavin reduction Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.15 7.5
-
-
Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.3.15 5 10 pH profiles, the enzyme shows a ping-pong bi-bi kinetic mechanism between pH 6.0 and 10.0, overview Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.15 flavin dependent on Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.3.15 280
-
chloride pH 7.0, 25°C Homo sapiens

General Information

EC Number General Information Comment Organism
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 Homo sapiens