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Information on EC 4.1.1.2 - oxalate decarboxylase and Organism(s) Bacillus subtilis and UniProt Accession O34767
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4.1.1.2 oxalate decarboxylaseIUBMB Comments
The enzyme from Bacillus subtilis contains manganese and requires O2 for activity, even though there is no net redox change.
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Word Map
- 4.1.1.2
- hyperoxaluria
- velutipes
-
oxalate-degrading
-
flammulina
-
mniii
-
mn-dependent
-
bicupins
-
collybia
- medicine
- agriculture
- paper production
- industry
- biotechnology
- degradation
- synthesis
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
oxalate decarboxylase, oxdc, oxazyme, oxdc-clec, fvoxdc, odc c, oxalate-decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, oxalate
-
-
-
-
oxazyme
-
oxazyme (OC4) is an orally administered formulation that has as an active component a recombinant mutant form of Bacillus subtilis oxalate decarboxylase (OxDC) enzyme C383S
OXD
-
-
-
-
OXDC
YvrK
additional information
OXDC
-
-
OXDC
-
additional information
enzyme belongs to the cupin superfamily, bicupin
additional information
the enzyme is a member of the cupin superfamily of proteins
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxalate + H+ = formate + CO2
detailed catalytic mechanism, kinetic mechanism
-
oxalate + H+ = formate + CO2
catalytic mechanism of oxalate decarboxylase compared to oxalate oxidase, EC 1.2.3.4
oxalate + H+ = formate + CO2
catalytic mechanism, the N-terminal Mn-binding site can mediate catalysis involving the important residue Asp92
-
oxalate + H+ = formate + CO2
minimal, two step kinetic mechanism for enzyme-catalyzed decarboxylation proton-coupled electron transfer and decarboxylation
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
oxalate carboxy-lyase (formate-forming)
The enzyme from Bacillus subtilis contains manganese and requires O2 for activity, even though there is no net redox change.
CAS REGISTRY NUMBER
COMMENTARY
9024-97-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxalate + H+
formate + CO2
oxalate-degrading enzyme
-
?
oxalate + H+
formate + CO2
oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton
-
?
Oxalate
Formate + CO2
-
the first two steps of the catalytic mechanism are reversible, the last step is irreversible
-
-
ir
oxalate + H+
formate + CO2
-
-
678138, 687082, 691955, 692903, 694237, 713879, 714726, 715299, 716726, 727124, 727707, 728195, 748313, 748822
-
-
?
oxalate + H+
formate + CO2
catalytic mechanism involves the requirement of an active site proton donor: Glu-162, catalytic cycle, enzyme structure, N-terminal domain is the catalytically active domain, dioxygen-dependent reaction involves no net redox change
-
?
oxalate + H+
formate + CO2
contains two potential active sites per subunit
-
?
oxalate + H+
formate + CO2
enzyme structure, YvrK possesses two potential active sites per subunit, but only one could be fully occupied by manganese, mechanism, catalytic cycle
-
?
oxalate + H+
formate + CO2
-
mechanism, multistep model in which a reversible, proton-coupled, electron transfer from bound oxalate to the Mn-enzyme gives an oxalate radical, which decarboxylates to yield a formate radical anion, subsequent reduction and protonation of this intermediate then gives formate, irreversible decarboxylation step, no net redox change between substrate and products, roles of Arg-270 and Glu-333 in catalysis
-
?
oxalate + H+
formate + CO2
OXDC acts exclusively on oxalate, Glu-333 of the second Mn-binding site serves as a proton donor in the production of formate, catalytic mechanism, enzyme structure
-
?
oxalate + H+
formate + CO2
involved in the elevation of cytoplasmic pH
-
?
oxalate + H+
formate + CO2
-
oxalate-degrading enzyme, possibly involved in decarboxylative phosphorylation, YvrK could contribute to the raising of cytoplasmic pH when the organism encounters low values of pH in soil and rotting vegetation
-
?
oxalate + H+
formate + CO2
-
regulation of OxdD synthesis and assembly in the spore coat, transcription of oxdD gene is induced during sporulation as a monocistronic unit under the control of sigmaK and is negatively regulated by GerE
-
?
oxalate + H+
formate + CO2
catalytic cycle involving radical formation with O2, overview, only Mn2+ binding site 1 is catalytically active, while Mn2+ binding site 2 is purely structural, overview
-
-
ir
oxalate + H+
formate + CO2
-
catalytic cycle, overview, the enzyme converts oxalate to formate and carbon dioxide, via an enzyme-bound formyl radical catalytic intermediate, and uses dioxygen as a cofactor despite the reaction involving no net redox change, overview, a proton transfer event occurs during a rate-limiting step, hydron exchange in formate, semiempirical quantum mechanical calculation, overview
-
-
?
additional information
?
-
enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations
-
?
additional information
?
-
enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations
-
?
additional information
?
-
-
enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations
-
?
additional information
?
-
enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations, at less than 1% of the oxalate decarboxylation rate
-
?
additional information
?
-
enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations, at less than 1% of the oxalate decarboxylation rate
-
?
additional information
?
-
-
enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations, at less than 1% of the oxalate decarboxylation rate
-
?
additional information
?
-
-
the enzyme also shows oxalate oxidase activity, catalytic cycle, overview
-
-
?
additional information
?
-
the enzyme also shows oxalate oxidase activity, catalytic cycle, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxalate + H+
formate + CO2
oxalate-degrading enzyme
-
?
oxalate + H+
formate + CO2
oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton
-
?
oxalate + H+
formate + CO2
-
-
-
-
?
oxalate + H+
formate + CO2
involved in the elevation of cytoplasmic pH
-
?
oxalate + H+
formate + CO2
-
oxalate-degrading enzyme, possibly involved in decarboxylative phosphorylation, YvrK could contribute to the raising of cytoplasmic pH when the organism encounters low values of pH in soil and rotting vegetation
-
?
oxalate + H+
formate + CO2
-
regulation of OxdD synthesis and assembly in the spore coat, transcription of oxdD gene is induced during sporulation as a monocistronic unit under the control of sigmaK and is negatively regulated by GerE
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
requirement, both Mn2+ and O2 are cofactors acting together as a two-electron sink during catalysis
O2
O2 might participate as a reversible electron sink in two putative proton-coupled electron transfer steps and is not merely used to generate a protein-based radical or oxidized metal center
O2
purified oxalate decarboxylase degrades more than 50% of oxalate when incubated with MnCl2 and sodium oxalate in atmospheric O2
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn3+
required for activity. Up to 16% of the electron paramagnetic resonance-visible manganese is in the +3 oxidation state at low pH in the presence of succinate buffer
additional information
Mn2+
contains 2 Mn2+ per subunit, role in catalysis, mechanism, 2 Mn-binding sites, the N-terminal Mn-binding site 1 is catalytically active
Mn2+
-
contains Mn2+ in its resting state and two Mn-binding sites, may be only the C-terminal binding site is catalytically active, the N-terminal site not, manganese in the active site can abstract an electron from bound substrate
Mn2+
metalloenzyme, Mn2+-dependent, each cupin domain contains one Mn-binding site that is buried deeply inside the beta-barrel, 2 binding sites within a monomer, mode of binding, mechanism
Mn2+
specific requirement for the correct folding and activity, contains between 0.86 and 1.14 atoms of manganese per subunit, predominantly in the Mn2+ oxidation state, both Mn2+ and O2 are cofactors acting together as a two-electron sink during catalysis
Mn2+
required, each subunit contains two similar, but distinct, manganese sites 1 and 2, only site 1 is catalytically active, and site 2 is purely structural, manganese content of mutant enzymes, overview
Mn2+
-
the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues, multifrequency EPR studies on the Mn2+ centers of oxalate decarboxylase, overview
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
Mn2+
two manganese binding sites, Glu162 on a flexible lid is the site 1 general acid, Mn2+ content of mutant enzymes, overview
Mn2+
-
His-tagged recombinant enzyme contains 1.2 Mn2+ per subunit, non-His-tagged recombinant enzyme contains 2.0 Mn2+ per subunit
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
Mn2+
dependent on, two Mn(II) centers located in the N- and C-terminal cupin domains of the enzyme, hydrogen bonding interaction between the side chains of a conserved Tryp132 and Glu101 coordinating Mn(II) in the N-terminal domain. Computational analysis of electronic properties of protein-bound Mn(II) ions using X-ray crystal protein structure with PDB ID 1UW8, quantum mechanical/molecular mechanical optimization and modeling, density functional theory and density functional theory/molecular mechanical calculations. Experimental and calculated fine structure parameters of wild-type and W132F mutant enzymes, overview
Mn2+
required, the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site
Mn2+
-
the enzyme has two domains, each containing a Mn(II) ion coordinated with three histidine residues, binding structure in domain I, overview
additional information
enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+
additional information
-
enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+
additional information
-
presence of a metal ion, role of a transition metal in catalysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dithionite
1 mM, complete loss of activity, some irreversible effect
nitric oxide
-
reversible inhibition under dioxygen-depleted conditions with 100fold reduction of activity in the presence of 0.05 mM nitric oxide. At 12 min, air is re-introduced, resulting in the restoration of full OxDC catalytic activity, albeit after a time lag of approximately 5 min
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
dioxygen-dependent reaction suggesting the role of a transition metal in catalysis
additional information
-
pH-dependent induction in acidic growth media, particularly at pH 5, but not by oxalate
-
additional information
-
overexpression of YvrI results in induction of OxdC transcription
-
additional information
-
OxdC is maximally expressed under acidic growth conditions (LB medium acidified to pH 5.4 with either phytate or HCl)
-
additional information
-
YvrI and its associated coregulators YvrHa and YvrL are required for the regulation of OxdC expression by acid stress
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
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
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
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
22.61
oxalate
-
Eupergit C-immobilized enzyme, citrate buffer (0.05 M, pH 4.0), at 37°C
additional information
additional information
-
kinetic data, kinetic mechanism
-
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
Fourier transform infrared spectroscopy to monitor in real time both substrate consumption and product formation, the Km for oxalate determined using this assay is 3.8fold lower than that estimated from a stopped assay, overview, solvent deuterium kinetic isotope effect, overview
-
additional information
additional information
kinetic analysis, different assay methods
-
additional information
additional information
-
steady-state kinetics of mutant enzyme, minimal kinetic model
-
additional information
additional information
steady-state kinetics of the T165S and T165V enzyme mutants, overview
-
additional information
additional information
-
steady-state kinetics of the T165S and T165V enzyme mutants, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
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
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
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
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
nitric oxide
-
apparent value, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
mutant enzyme T165S, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
29
mutant enzyme S161T, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
4.5
mutant enzyme T165V, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
40
48
mutant enzyme S161A, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
additional information
40
wild type enzyme, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
additional information
activity of recombinant wild-type and mutant enzymes, overview
additional information
-
two assay methods, stopped assay and Fourier transform infrared spectroscopy to monitor in real time both substrate consumption and product formation
additional information
-
specific activity of oxalate decarboxylase in crude cell-free extract of recombinant Lactobacillus plantarum NC8 and Escherichia coli (pLB36) compared with wild-type Lactobacillus plantarum NC8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 5
-
soluble and immobilized enzyme. When decreasing pH to 3.0, the soluble enzyme loses 76% of its original activity, but there is only 41% loss for the immobilized enzyme
3 - 7.5
4 - 6
-
the enzyme activity is increased 4.4times when the pH increases from 4.0 to the optimum pH of 5.5. When pH increases from 5.5 to 6.0, enzyme activity is reduced 0.02times
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
26
37
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
the soluble enzyme shows at least more than 50% activity between 30 and 70°C. The immobilized enzyme almost retains its full maximum activity at 70°C (7% decrease of activity), while the soluble enzyme shows about 50% activity at 70°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
recombinant enzyme mutant T165V has two isoelectric points at pH 4.2 and pH 5.7
5.1
5.7
recombinant enzyme mutant T165V has two isoelectric points at pH 4.2 and pH 5.7
6.1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the accumulation of OxdC in the cell wall proteome under acidic growth conditions is absolutely dependent on YvrI
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
analysis of transport of the product, i.e., CO2, from the reaction center to the surface of the enzyme using atomistic molecular dynamics simulations. Structure-function analysis using protein crystal structure, PDB ID 1L3J, simulations, overview. Domain I is the active site domain, while domain II is nonreceptive to hosting the formate and is incapable of releasing the CO2 molecule
additional information
the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site of Bacillus subtilis oxalate decarboxylase. O2 might participate as a reversible electron sink in two putative proton-coupled electron transfer steps and is not merely used to generate a protein-based radical or oxidized metal center. The conserved Arg/Thr hydrogen bond is important for correctly locating the side chain of Glu162, which mediates a proton-coupled electron transfer step prior to decarboxylation in the catalytically competent form of the enzyme
additional information
-
the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site of Bacillus subtilis oxalate decarboxylase. O2 might participate as a reversible electron sink in two putative proton-coupled electron transfer steps and is not merely used to generate a protein-based radical or oxidized metal center. The conserved Arg/Thr hydrogen bond is important for correctly locating the side chain of Glu162, which mediates a proton-coupled electron transfer step prior to decarboxylation in the catalytically competent form of the enzyme
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
43407
-
5 * 44000, SDS-PAGE, 5 * 43407, calculated from the amino acid sequence, pentamer, but it is possible, that YvrK is actually a hexamer
44000
44000
-
5 * 44000, SDS-PAGE, 5 * 43407, calculated from the amino acid sequence, pentamer, but it is possible, that YvrK is actually a hexamer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
pentamer
-
5 * 44000, SDS-PAGE, 5 * 43407, calculated from the amino acid sequence, pentamer, but it is possible, that YvrK is actually a hexamer
additional information
hexamer
homohexamer, each subunit contains two similar, but distinct, manganese sites, only site 1 is catalytically active and site 2 is purely structural
hexamer
-
functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits
additional information
-
the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified His6-tagged enzyme mutant T165V, sitting drop vapor diffusion method, mixing of 0.0012 ml of 6 mg/mL protein in 1 mM HEPES buffer, pH 7.5, with 0.0012 ml of precipitant solution containing 10% w/v PEG 6000 and 2 M NaCl, and equilibration against well solution, 17°C, 1 week, X-ray diffraction structure determination and analysis at 2.31 A resolution
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
purified recombinant His6-tagged Mn(II)-substituted W132F enzyme mutant, hanging drop vapour diffusion method, mixing of 0.002 ml of 5 mg/ml protein in 100 mM Tris-HCl, pH 8.5, and 500 mM NaCl with.0.002 ml of well solution containing 100 mM Tris-HCl, pH 8.5, 2 M NaCl, and 10% PEG 6000, 17°C, 2 months, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution
purified recombinant mutants R92A, DELTA162-163, S161A, and E162A, hanging-drop vapour diffusion method at 18°C, the mutants enzymes generally crystallize with 8-15% v/v PEG 8000, 0.1 M Tris, pH 8.5, and 0-15% xylitol, further method optimization for each mutant enzyme, X-ray diffraction structure determination and analysis at 2.0-3.1 A resolution, molecular modelling
recombinant OXDC, 3-dimensional structures in absence of formate and complexed with formate, hanging drop vapor diffusion technique, X-ray analysis
recombinant OxdC, hanging drop vapour diffusion method, X-ray analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D297A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
E162A
E162A/N163S/S164N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E162D
E162Q
E162Q/E333Q
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
E333A
E333D
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
E333Q
E33D
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H299A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R270A
R270K
R270Q
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R92A
R92K
R92K/R270K
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
S161A
S161D/E162A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S161D/E162A/N163S/S164N
site-directed mutagenesis, almost inactive mutant
S161D/E162A/N163S/S164N/T165Q
site-directed mutagenesis, almost inactive mutant
S161D/E162S/N163S/S164N
site-directed mutagenesis, almost inactive mutant
S161D/N163S/S164N
site-directed mutagenesis, the mutant shows about 60% reduced activity compared to the wild-type enzyme
S161T
the mutant shows reduced specific activity compared to the wild type enzyme
S164A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
T165P
site-directed mutagenesis, altered comformation with dominant conformation of the lid compared to the wild-type enzyme
T165S
T165V
W132F
additional information
E162A
site-directed mutagenesis, the mutant lacks both oxalate decarboxylase and oxalate oxidase activities, structure analysis
E162D
site-directed mutagenesis, E162D mutant retains 29% of the decarboxylase activity compared to the wild-type enzyme
E162D
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and slightly reduced activity compared to the wild-type enzyme
E162Q
Mn2+-binding site 1 mutant, Vmax and kcat/Km is 1% that of wild-type
E162Q
site-directed mutagenesis, E162Q mutant retains only 1% of the decarboxylase activity compared to the wild-type enzyme
E162Q
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
E333A
Mn2+-binding site 2 mutant, 4-6% of wild-type activity at pH 4, lower Km for oxalate, kcat/Km is 25% that of wild-type
E333A
mutant of the Mn-binding site in domain II, 25fold reduced formate production, 4fold reduced CO2 production
E333A
site-directed mutagenesis, the mutant shows reduced oxalate decarboxylase and oxalate oxidase activities compared to the wild-type enzyme
E333Q
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
E333Q
site-directed mutagenesis, the mutant lacks both oxalate decarboxylase and oxalate oxidase activities
R270A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R270K
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
R92A
site-directed mutagenesis, the mutant lacks both oxalate decarboxylase and oxalate oxidase activities, structure analysis
R92K
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
R92K
site-directed mutagenesis, the mutant lacks both oxalate decarboxylase and oxalate oxidase activities
S161A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme, structure analysis
S161A
the mutant shows increased specific activity compared to the wild type enzyme
T165S
the mutant shows reduced specific activity compared to the wild type enzyme
T165S
site-directed mutagenesis, the T165S enzyme variant exhibits similar catalytic activity to wild-type enzyme when adjusted for the amount of Mn(II) incorporated into the recombinant protein
T165V
the mutant shows strongly reduced specific activity compared to the wild type enzyme
T165V
site-directed mutagenesis, removal a conserved Arg/Thr hydrogen bonding interaction, the mutant exhibits impaired catalytic activity. The T165V OxDC variant exhibits a 15fold reduced catalytic efficiency and a lower level of oxalate consumption per dioxygen molecule compared to the wild-type
T165V
the catalytic efficiency for decarboxylase activity in the mutant is approximately ten times lower than in wild type
W132F
site-directed mutagenesis, the mutation causes structural changes in the N-terminal and C-terminal metal center, superimposing of the X-ray crystal structures of the Mn-containing wild-type enzyme, PDB ID 1UW8, and the Co-containing W132F enzyme mutant
W132F
the mutant with increased manganese content shows reduced activity compared to the wild type enzyme
additional information
-
oxdD insertional mutant AH2898 missing OxdD protein
additional information
construction of deletion mutant DELTA162-163 or inactive deletion mutant DELTA162-164, structure analysis, manganese content of mutant enzymes, overview
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
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
additional information
-
mutation of Glu 333 present in domain II leads to a reduction in the activity of the enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
-
both the soluble and immobilized enzyme are stable after 6 h of treatment with buffer at a pH higher than 4.5, and no obvious activity decrease are observed. There is 36.9% activity preserved in the immobilized enzyme after 6 h of treatment with a pH 3.5 buffer, and 4.2% activity remains in the soluble enzyme
716726
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 70
-
both soluble and immobilized enzyme lose their activity continuously at 60°C treatment (1 h at pH 4.0). After thermal treatment for 10 min, 46.07% activity remains for the immobilized enzyme an keep 13.86% activity after 1 h of thermal treatment, while the soluble one loses its activity completely
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
under the condition of enzyme/support ratio at 1:20, pH 9, with 1.5 M (NH4)2SO4, 22°C, and shaking at 30 rpm for 24 h, activity recovery of Eupergit C-immobilized enzyme reaches 90%
-
unstable enzyme, loses activity during purification, undergoes partial precipitation during assays
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
YvrK is occasionally prone to oxidation during the latter stages of the purification resulting in its dimerization, which is prevented by dithiothreitol
652196
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
Ni-NTA column chromatography
recombinant C-terminally His-tagged OxdC from Escherichia coli strain BL21(DE3)
-
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant C-terminally His6-tagged enzyme mutants T165V and T165S by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Lactobacillus plantarum strain WCFS1 supernatant by ammonium sulfate fractionation, affinity chromatography, and dialysis
-
recombinant His6-tagged Mn(II)-substituted W132F enzyme mutant by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant OXDC
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene oxdC, cloning and expression in Escherichia coli strain DH5alpha and BL21(DE3), constitutive overexpression from plasmid pLB36, with promoter PldhL from Lactobacillus plantarum NCIMB8826, in Lactobacillus plantarum strain NC8. The recombinant Lactobacillus plantarum is able to degrade more than 90% of added oxalate, compared to 15% by the wild-type, and also shows higher tolerance to oxalate
-
gene oxdC, cloning in Escherichia coli strain DH10B, functional overexpression of His-tagged enzyme in Lactobacillus plantarum strain WCFS1, isolated from human saliva, using homologous signal peptides Lp 0373 and Lp 3050, the recombinant strain secretes the recombinant protein. The recombinant Lactobacillus plantarum harboring pLp 0373sOxdC and pLp 3050sOxdC can express and secrete functional OxdC and degrade oxalate up to 50% and 30%, respectively
-
gene oxdC, expression of C-terminally His-tagged OxdC in Escherichia coli strain BL21(DE3)
-
gene oxdC, expression of the C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene oxdC, expression of the C-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
gene oxdC, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
oxdD gene, expression in Escherichia coli, genetic organization of the oxdD locus
-
recombinant expression of C-terminally His6-tagged wild-type enzyme and mutants T165V and T165S, expression is induced in the presence of 5 mM MnCl2 after heat shocking the bacteria for 18 min at 42°C
recombinant expression of His6-tagged Mn(II)-substituted W132F enzyme mutant
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
YvrI is essential for acid stress induction of oxdC transcription, YvrI and YvrL regulate OxdC accumulation in response to acid stress
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
treatment of hyperoxaluria, urolithiasis, nephrocalcinosis, and depletion of dietary oxalate with enzyme formulation
medicine
-
the transgenic Lactobacillus plantarum strain WCFS1 expressing the enzyme from Bacillus subtilis may provide possible therapeutic approach by degrading intestinal oxalate in the human host of Lactobacillus plantarum
medicine
-
HEK-293 cells expressing the enzyme capable of degrading oxalate protect cells from oxidative damage and thus serve as a therapeutic option for prevention of calcium oxalate stone disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anand, R.; Dorrestein, P.C.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution
Biochemistry
41
7659-7669
2002
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 168 / CU1065 (O34714)
Reinhardt, L.A.; Svedruzic, D.; Chang, C.H.; Cleland, W.W.; Richards, N.G.J.
Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis
J. Am. Chem. Soc.
125
1244-1252
2003
Bacillus subtilis, Bacillus subtilis 168
Tanner, A.; Bornemann, S.
Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase
J. Bacteriol.
182
5271-5273
2000
Bacillus subtilis, Bacillus subtilis 168
Costa, T.; Steil, L.; Martins, L.O.; Volker, U.; Henriques, A.O.
Assembly of an oxalate decarboxylase produced under sigmaK control into the Bacillus subtilis spore coat
J. Bacteriol.
186
1462-1474
2004
Bacillus subtilis
Tanner, A.; Bowater, L.; Fairhurst, S.A.; Bornemann, S.
Oxalate decarboxylase requires manganese and dioxygen for activity. Overexpression and characterization of Bacillus subtilis YvrK and YoaN
J. Biol. Chem.
276
43627-43634
2001
Bacillus subtilis (O34714), Bacillus subtilis (O34767), Bacillus subtilis, Bacillus subtilis 168 (O34714), Bacillus subtilis 168 (O34767)
Just, V.J.; Stevenson, C.E.M.; Bowater, L.; Tanner, A.; Lawson, D.M.; Bornemann, S.
A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site
J. Biol. Chem.
279
19867-19874
2004
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 168 (O34714)
Chang, C.H.; Svedruzic, D.; Ozarowski, A.; Walker, L.; Yeagle, G.; Britt, R.D.; Angerhofer, A.; Richards, N.G.
EPR spectroscopic characterization of the manganese center and a free radical in the oxalate decarboxylase reaction: identification of a tyrosyl radical during turnover
J. Biol. Chem.
279
52840-52849
2004
Bacillus subtilis
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
Arch. Biochem. Biophys.
464
36-47
2007
Bacillus subtilis
Just, V.J.; Burrell, M.R.; Bowater, L.; McRobbie, I.; Stevenson, C.E.; Lawson, D.M.; Bornemann, S.
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations
Biochem. J.
407
397-406
2007
Bacillus subtilis (O34714), Bacillus subtilis 168 (O34714)
Muthusamy, M.; Burrell, M.R.; Thorneley, R.N.; Bornemann, S.
Real-time monitoring of the oxalate decarboxylase reaction and probing hydron exchange in the product, formate, using fourier transform infrared spectroscopy
Biochemistry
45
10667-10673
2006
Bacillus subtilis
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
Biochemistry
46
12327-12336
2007
Bacillus subtilis (O34714), Bacillus subtilis
Angerhofer, A.; Moomaw, E.W.; Garcia-Rubio, I.; Ozarowski, A.; Krzystek, J.; Weber, R.T.; Richards, N.G.
Multifrequency EPR studies on the Mn(II) centers of oxalate decarboxylase
J. Phys. Chem. B
111
5043-5046
2007
Bacillus subtilis
Scarpellini, M.; Gaetjens, J.; Martin, O.J.; Kampf, J.W.; Sherman, S.E.; Pecoraro, V.L.
Modeling the resting state of oxalate oxidase and oxalate decarboxylase enzymes
Inorg. Chem.
47
3584-3593
2008
Bacillus subtilis, Thermotoga maritima
Kolandaswamy, A.; George, L.; Sadasivam, S.
Heterologous expression of oxalate decarboxylase in Lactobacillus plantarum NC8
Curr. Microbiol.
58
117-121
2009
Bacillus subtilis
MacLellan, S.R.; Helmann, J.D.; Antelmann, H.
The YvrI alternative sigma factor is essential for acid stress induction of oxalate decarboxylase in Bacillus subtilis
J. Bacteriol.
191
931-939
2009
Bacillus subtilis, Bacillus subtilis 168 / CU1065
MacLellan, S.R.; Wecke, T.; Helmann, J.D.
A previously unidentified sigma factor and two accessory proteins regulate oxalate decarboxylase expression in Bacillus subtilis
Mol. Microbiol.
69
954-967
2008
Bacillus subtilis, Bacillus subtilis 168 / CU1065
Moomaw, E.W.; Angerhofer, A.; Moussatche, P.; Ozarowski, A.; Garcia-Rubio, I.; Richards, N.G.
Metal dependence of oxalate decarboxylase activity
Biochemistry
48
6116-6125
2009
Bacillus subtilis (O34714), Bacillus subtilis
Cowley, A.B.; Poage, D.W.; Dean, R.R.; Meschter, C.L.; Ghoddusi, M.; Li, Q.S.; Sidhu, H.
14-day repeat-dose oral toxicity evaluation of oxazyme in rats and dogs
Int. J. Toxicol.
29
20-31
2010
Bacillus subtilis
Tabares, L.C.; Gaetjens, J.; Hureau, C.; Burrell, M.R.; Bowater, L.; Pecoraro, V.L.; Bornemann, S.; Un, S.
pH-Dependent structures of the manganese binding sites in oxalate decarboxylase as revealed by high-field electron paramagnetic resonance
J. Phys. Chem. B
113
9016-9025
2009
Bacillus subtilis
Maekelae, M.R.; Hilden, K.; Lundell, T.K.
Oxalate decarboxylase: biotechnological update and prevalence of the enzyme in filamentous fungi
Appl. Microbiol. Biotechnol.
87
801-814
2010
Agaricus bisporus, Aspergillus niger, Aspergillus sp., Bacillus subtilis, Dichomitus squalens, Flammulina sp., Flammulina sp. IJF 140502, Flammulina velutipes, Pandorea sp., Pandorea sp. OXJ-11a, Phanerodontia chrysosporium, Trametes versicolor
Moral, M.E.; Tu, C.; Imaram, W.; Angerhofer, A.; Silverman, D.N.; Richards, N.G.
Nitric oxide reversibly inhibits Bacillus subtilis oxalate decarboxylase
Chem. Commun. (Camb. )
47
3111-3113
2011
Bacillus subtilis
Imaram, W.; Saylor, B.T.; Centonze, C.P.; Richards, N.G.; Angerhofer, A.
EPR spin trapping of an oxalate-derived free radical in the oxalate decarboxylase reaction
Free Radic. Biol. Med.
50
1009-1015
2011
Bacillus subtilis (O34714), Bacillus subtilis
Wolfenden, R.; Lewis, C.A.; Yuan, Y.
Kinetic challenges facing oxalate, malonate, acetoacetate, and oxaloacetate decarboxylases
J. Am. Chem. Soc.
133
5683-5685
2011
Bacillus subtilis
Lin, R.; Wu, R.; Huang, X.; Xie, T.
Immobilization of oxalate decarboxylase to Eupergit and properties of the immobilized enzyme
Prep. Biochem. Biotechnol.
41
154-165
2011
Bacillus subtilis
Saylor, B.T.; Reinhardt, L.A.; Lu, Z.; Shukla, M.S.; Nguyen, L.; Cleland, W.W.; Angerhofer, A.; Allen, K.N.; Richards, N.G.
A structural element that facilitates proton-coupled electron transfer in oxalate decarboxylase
Biochemistry
51
2911-2920
2012
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 168 (O34714)
Sasikumar, P.; Gomathi, S.; Anbazhagan, K.; Selvam, G.S.
Secretion of biologically active heterologous oxalate decarboxylase (OxdC) in Lactobacillus plantarum WCFS1 using homologous signal peptides
BioMed Res. Int.
2013
280432
2013
Bacillus subtilis
Campomanes, P.; Kellett, W.F.; Easthon, L.M.; Ozarowski, A.; Allen, K.N.; Angerhofer, A.; Rothlisberger, U.; Richards, N.G.
Assigning the EPR fine structure parameters of the Mn(II) centers in Bacillus subtilis oxalate decarboxylase by site-directed mutagenesis and DFT/MM calculations
J. Am. Chem. Soc.
136
2313-2323
2014
Bacillus subtilis (O34714), Bacillus subtilis
Anbazhagan, K.; Sasikumar, P.; Gomathi, S.; Priya, H.P.; Selvam, G.S.
In vitro degradation of oxalate by recombinant Lactobacillus plantarum expressing heterologous oxalate decarboxylase
J. Appl. Microbiol.
115
880-887
2013
Bacillus subtilis
Karmakar, T.; Periyasamy, G.; Balasubramanian, S.
CO2 migration pathways in oxalate decarboxylase and clues about its active site
J. Phys. Chem. B
117
12451-12460
2013
Bacillus subtilis
Twahir, U.T.; Ozarowski, A.; Angerhofer, A.
Redox cycling, pH dependence, and ligand effects of Mn(III) in oxalate decarboxylase from Bacillus subtilis
Biochemistry
55
6505-6516
2016
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 168 (O34714)
Zhu, W.; Reinhardt, L.A.; Richards, N.G.J.
Second-shell hydrogen bond impacts transition-state structure in Bacillus subtilis oxalate decarboxylase
Biochemistry
57
3425-3432
2018
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 168 (O34714)
Lee, E.; Jeong, B.C.; Park, Y.H.; Kim, H.H.
Expression of the gene encoding oxalate decarboxylase from Bacillus subtilis and characterization of the recombinant enzyme
BMC Res. Notes
7
598
2014
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 128 (O34714)
Twahir, U.T.; Stedwell, C.N.; Lee, C.T.; Richards, N.G.; Polfer, N.C.; Angerhofer, A.
Observation of superoxide production during catalysis of Bacillus subtilis oxalate decarboxylase at pH 4
Free Radic. Biol. Med.
80
59-66
2015
Bacillus subtilis (O34714), Bacillus subtilis, Bacillus subtilis 168 (O34714)
Albert, A.; Tiwari, V.; Paul, E.; Ganesan, D.; Ayyavu, M.; Kujur, R.; Ponnusamy, S.; Shanmugam, K.; Saso, L.; Govindan Sadasivam, S.
Expression of heterologous oxalate decarboxylase in HEK293 cells confers protection against oxalate induced oxidative stress as a therapeutic approach for calcium oxalate stone disease
J. Enzyme Inhib. Med. Chem.
32
426-433
2017
Bacillus subtilis
Koni, T.; Rusma, R.; Hanim, C.; Zupriza, Z.
Effect of pH and temperature on Bacillus subtilis FNCC 0059 oxalate decarboxylase activity
Pak. J. Biol. Sci.
20
436-441
2017
Bacillus subtilis, Bacillus subtilis FNCC 0059
-
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