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Literature summary for 1.1.3.15 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

Application Comment Organism
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

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

Inhibitors

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UJM8
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glycolate oxidase
-
Homo sapiens
GOX
-
Homo sapiens

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
15.7
-
glycolate pH 7.0, 30°C, recombinant enzyme, first order Homo sapiens
20
-
glycolate pH 7.5, 30°C, recombinant enzyme, first order Homo sapiens
31.2
-
glycolate pH 9.0, 30°C, recombinant enzyme, first order Homo sapiens
54.1
-
flavin pH 7.0, 30°C, flavin reduction Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
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

Cofactor Comment Organism Structure
flavin dependent on Homo sapiens

Ki Value [mM]

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

General Information

General Information Comment Organism
malfunction the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones Homo sapiens