Literature summary for 4.1.1.2 extracted from

Burrell, M.R.; Just, V.J.; Bowater, L.; Fairhurst, S.A.; Requena, L.; Lawson, D.M.; Bornemann, S.
Oxalate decarboxylase and oxalate oxidase activities can be interchanged with a specificity switch of up to 282,000 by mutating an active site lid (2007), Biochemistry, 46, 12327-12336.

Cloned(Commentary)

Cloned (Comment)	Organism
gene oxdC, expression of the C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging drop vapor diffusion method, 0.001 m1 of 10 mg ml protein in 50 mM Tris-HCl, pH 8.5, containing 500 mM NaCl mixed with 0.001 ml of precipitant containing 4.5% w/v PEG 2000, 100 mM Tris-HCl, pH 8.5, 100 mM glycine, 5 mM DTT, and 0.5 mM MnCl2, suspended over 1 ml of precipitant at 18 °C, crystal cryoprotection by crystallization solution containing 25% w/v glycerol, X-ray diffraction structure determination and analysis at 1.80 A resolution, modelling	Bacillus subtilis

Crystallization (Comment)

Organism

purified recombinant enzyme, hanging drop vapor diffusion method, 0.001 m1 of 10 mg ml protein in 50 mM Tris-HCl, pH 8.5, containing 500 mM NaCl mixed with 0.001 ml of precipitant containing 4.5% w/v PEG 2000, 100 mM Tris-HCl, pH 8.5, 100 mM glycine, 5 mM DTT, and 0.5 mM MnCl2, suspended over 1 ml of precipitant at 18 °C, crystal cryoprotection by crystallization solution containing 25% w/v glycerol, X-ray diffraction structure determination and analysis at 1.80 A resolution, modelling

Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
E162A/N163S/S164N	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	Bacillus subtilis
additional information	the decarboxylase can be converted into an oxidase by mutating amino acids of the Mn2+-binding lid that include Glu162 with specificity switches, Mn2+ content of mutant enzymes, overview	Bacillus subtilis
S161D/E162A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	Bacillus subtilis
S161D/E162A/N163S	site-directed mutagenesis, almost inactive mutant	Bacillus subtilis
S161D/E162A/N163S/S164N	site-directed mutagenesis, almost inactive mutant	Bacillus subtilis
S161D/E162A/N163S/S164N/T165Q	site-directed mutagenesis, almost inactive mutant	Bacillus subtilis
S161D/E162S/N163S/S164N	site-directed mutagenesis, almost inactive mutant	Bacillus subtilis
S161D/N163S/S164N	site-directed mutagenesis, the mutant shows about 60% reduced activity compared to the wild-type enzyme	Bacillus subtilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	kinetics of recombinant wild-type and mutant enzymes, overview	Bacillus subtilis
2	-	oxalate	pH 4.0, recombinant mutant E162A/N163S/S164N	Bacillus subtilis
6.6	-	oxalate	pH 4.0, recombinant wild-type enzyme	Bacillus subtilis
9.1	-	oxalate	pH 4.0, recombinant mutant S161D/E162A	Bacillus subtilis
97	-	oxalate	pH 4.0, recombinant mutant S161D/N163S/S164N	Bacillus subtilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	two manganese binding sites, Glu162 on a flexible lid is the site 1 general acid, Mn2+ content of mutant enzymes, overview	Bacillus subtilis

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O34714	gene oxdC	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Bacillus subtilis

Reaction

Reaction	Comment	Organism	Reaction ID
oxalate = formate + CO2	catalytic mechanism of oxalate decarboxylase compared to oxalate oxidase, EC 1.2.3.4	Bacillus subtilis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Oxalate	-	Bacillus subtilis	Formate + CO2	-	?

Synonyms

Synonyms	Comment	Organism
More	the enzyme is a member of the cupin superfamily of proteins	Bacillus subtilis
OXDC	-	Bacillus subtilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4	-	assay at	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
O2	-	Bacillus subtilis