Literature summary for 4.1.1.2 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.

Search for more literature for 4.1.1.2

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	steady-state kinetics of mutant enzyme, minimal kinetic model	Bacillus subtilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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)

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	gene oxdC	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
OXDC	-	Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
23	-	assay at	Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.3	-	oxalate	pH 4.2, 23C, mutant E162Q	Bacillus subtilis
0.9	-	oxalate	pH 4.2, 23C, mutant R92K	Bacillus subtilis
29	-	oxalate	pH 4.2, 23C, mutant E162D	Bacillus subtilis
57	-	oxalate	pH 4.2, 23C, wild-type enzyme	Bacillus subtilis

pH Optimum

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

pH Range

pH Minimum	pH Maximum	Comment	Organism
4.2	6.7	-	Bacillus subtilis

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Release 2023.1 (January 2023)