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Literature summary extracted from

  • Whittaker, M.M.; Pan, H.Y.; Yukl, E.T.; Whittaker, J.W.
    Burst kinetics and redox transformations of the active site manganese ion in oxalate oxidase: Implications for the catalytic mechanism (2007), J. Biol. Chem., 282, 7011-7023.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.3.4 recombinant barley oxalate oxidase expressed in Pichia pastoris (X33) Hordeum vulgare

Protein Variants

EC Number Protein Variants Comment Organism
1.2.3.4 S49A nonglycosylated oxalate oxidase is produced by site-directed mutagenesis (S49A) Hordeum vulgare

General Stability

EC Number General Stability Organism
1.2.3.4 based on the absoption changes at 325 nm, it is possible to estimate the half-life of the Mn5+ species at room temperature: t1/2 = 42 h (pH 4) or 95 h (pH 7) Hordeum vulgare

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.3.4 additional information the presence of either superoxide dismutase or manganese catalase in the assay mixture dramatically accelerates turnover inactivation and resultes in a vanishingly small Vs value in the steady state Hordeum vulgare

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.3.4 0.78
-
oxalate oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25°C). The Km evalutated from initial velocity data exhibits a strong pH dependence with limiting slopes (versus pH) of 0.9 (below pH 4) and 1.5 (above pH 4) Hordeum vulgare

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.3.4 Mn2+ titration of periodate-oxidized oxalate oxidase with hydroxylamine completely eliminates the visible absorption, forming a homogeneous Mn2+ form of the enzyme. The fully reduced Mn2+ form lacks any detectable oxidase activity, reoxidation substantially restores the maximum activity. Hordeum vulgare
1.2.3.4 Mn3+ treatment of the periodate-oxidized enzyme with ascorbate results in a substantioal decrease in absorption, forming a complex that is spectroscopically identified as a Mn3+ species. Mn3+ form has a 5fold higher specific activity than native recombinant oxalate oxidase. Hordeum vulgare
1.2.3.4 Mn5+ titration of oxalate oxidase with sodium periodate results in nearly stoichometric oxidation of the enzyme to an intensely colored yellow complex, whose complete spectroscopic characterization lead to assignment to a superoxidized Mn5+ complex. Treatment of Mn2+ S49A oxalate oxidase generates the same yellow species as the glycosylated wild type enzyme. Mass spectra of isolated and periodate-treated oxalate oxidase are virtually identical, demonstating that no protein oxidation occurred. Peroxidate oxidation increases the specific activity about 5fold. Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.4 Hordeum vulgare
-
barley
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.3.4
-
Hordeum vulgare

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.3.4 additional information
-
the effect of the isotopic composition of the solvent is investigated by assaying oxalate oxidase in buffer prepared form H2O/D20 mixtures.The limiting values of Vs (steady state rate) lead to an estimate of the overall solvent kinetic isotope effect kH2O/kD2O = 8.5 (k=burst rate constant) Hordeum vulgare
1.2.3.4 additional information
-
Vimax (initial maximum velocity) is nearly independent of pH over the range from pH 3 to 5 Hordeum vulgare
1.2.3.4 21.9
-
native wild type oxalate oxidase Hordeum vulgare
1.2.3.4 94
-
native S49A oxalate oxidase Hordeum vulgare
1.2.3.4 139
-
periodate-oxidized oxalate oxidase, Mn5+ content 100% Hordeum vulgare
1.2.3.4 156
-
ascorbate-reduced oxalate oxidase, Mn3+ content above 95% Hordeum vulgare

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.3.4 9.7
-
oxalate oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25°C) Hordeum vulgare

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.3.4 2.5 6 the catalytic efficiency (Vmax/Km) increases continuously to lower pH Hordeum vulgare