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Literature summary for 4.1.1.2 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
Search for more literature for 4.1.1.2

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
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
-
 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
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
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
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

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Bacillus subtilis O34714
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
OXDC
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
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
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
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
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
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
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
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]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
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
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
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
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
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
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
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
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