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Literature summary extracted from

  • Svedruzic, D.; Liu, Y.; Reinhardt, L.A.; Wroclawska, E.; Cleland, W.W.; Richards, N.G.
    Investigating the roles of putative active site residues in the oxalate decarboxylase from Bacillus subtilis (2007), Arch. Biochem. Biophys., 464, 36-47.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.2 gene oxdC, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.2 E162D site-directed mutagenesis, the mutant enzyme shows altered kinetics and slightly reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 E162Q site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 E162Q/E333Q site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 E333D site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 E333Q site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 R270K site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 R92K site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 R92K/R270K site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.2 additional information
-
 additional information steady-state kinetics of mutant enzyme, minimal kinetic model 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 Mn(II) coordinated by four conserved residues Arg92, Arg270, Glu162, and Glu333, the N-terminal Mn-binding site can mediate catalysis Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.2 Oxalate Bacillus subtilis
-
 Formate + CO2
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Bacillus subtilis
-
 gene oxdC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.2 recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.2 oxalate = formate + CO2 catalytic mechanism, the N-terminal Mn-binding site can mediate catalysis involving the important residue Asp92 Bacillus subtilis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.2 0.4
-
 purified recombinant mutants R92K/R270K, E162Q and E333Q Bacillus subtilis
4.1.1.2 0.7
-
 purified recombinant mutant E162Q/E333Q Bacillus subtilis
4.1.1.2 1.3
-
 purified recombinant mutant R92K Bacillus subtilis
4.1.1.2 2.4
-
 purified recombinant mutant R270K Bacillus subtilis
4.1.1.2 4
-
 purified recombinant mutant E333D Bacillus subtilis
4.1.1.2 30 72 purified wild-type enzyme, dependent on purification procedure Bacillus subtilis
4.1.1.2 40
-
 purified recombinant mutant E162D Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 Oxalate
-
 Bacillus subtilis Formate + CO2
-
 ir
4.1.1.2 Oxalate the first two steps of the catalytic mechanism are reversible, the last step is irreversible Bacillus subtilis Formate + CO2
-
 ir

Subunits

EC Number Subunits Comment Organism
4.1.1.2 More the enzyme is composed of two cupin domains Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 OXDC
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.2 23
-
 assay at 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 0.3
-
 oxalate pH 4.2, 23C, mutant E162Q Bacillus subtilis
4.1.1.2 0.9
-
 oxalate pH 4.2, 23C, mutant R92K Bacillus subtilis
4.1.1.2 29
-
 oxalate pH 4.2, 23C, mutant E162D Bacillus subtilis
4.1.1.2 57
-
 oxalate pH 4.2, 23C, wild-type enzyme Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.2 4.2
-
 assay at Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.2 4.2 6.7
-
 Bacillus subtilis