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Literature summary extracted from

  • Moomaw, E.W.; Angerhofer, A.; Moussatche, P.; Ozarowski, A.; Garcia-Rubio, I.; Richards, N.G.
    Metal dependence of oxalate decarboxylase activity (2009), Biochemistry, 48, 6116-6125.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.2 expressed in Escherichia coli BL21(DE3) cells Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.2 E101A the mutant shows strongly decreased activity Bacillus subtilis
4.1.1.2 E101D the mutant shows strongly decreased activity Bacillus subtilis
4.1.1.2 E101Q the mutant shows strongly decreased activity Bacillus subtilis
4.1.1.2 E101Q/E280Q the mutant shows strongly decreased activity Bacillus subtilis
4.1.1.2 E280A the mutant shows strongly decreased activity Bacillus subtilis
4.1.1.2 E280D the mutant shows strongly decreased activity Bacillus subtilis
4.1.1.2 E280Q the mutant shows strongly decreased activity Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.2 2.9
-
oxalate mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 2.9
-
oxalate mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 3
-
oxalate mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 3.4
-
oxalate mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 4
-
oxalate mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 5.4
-
oxalate mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 8.4
-
oxalate wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 10.1
-
oxalate mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion, OxDC activity is linearly correlated with manganese content, untagged enzyme samples exhibit a metal content of 1.8 Mn2+ per monomer Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Bacillus subtilis O34714
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.2 DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 oxalate + H+
-
Bacillus subtilis CO2 + formate
-
?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 OXDC
-
Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.2 0.012
-
oxalate mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.019
-
oxalate mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.046
-
oxalate mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.14
-
oxalate mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.49
-
oxalate mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.62
-
oxalate mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.62
-
oxalate mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 53
-
oxalate wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.2 0.004
-
oxalate mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.006
-
oxalate mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.016
-
oxalate mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.026
-
oxalate mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.061
-
oxalate mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.144
-
oxalate mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 0.155
-
oxalate mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis
4.1.1.2 6.309
-
oxalate wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C Bacillus subtilis