Information on EC 4.1.1.2 - oxalate decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.1.1.2
-
RECOMMENDED NAME
GeneOntology No.
oxalate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
oxalate + H+ = formate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
-
-
Metabolic pathways
-
-
oxalate degradation V
-
-
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 hide
9024-97-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain C58
-
-
Manually annotated by BRENDA team
strain C58
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PO114, white rot fungus
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Ceriporiopsis subvermispora
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Ceriporiopsis subvermispora CZ-3
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Haploporus odorus strain T154
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Nematoloma frowardii
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Nematoloma frowardii b19
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Phanerochaete chrysosporium
ATCC 24725, white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Phanerochaete chrysosporium F1767
ATCC 24725, white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Phlebiopsis gigantea
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Phlebiopsis gigantea T55
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Radulodon erikssonii
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Radulodon erikssonii T84
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Solanum lycopersicum
in fruits
-
-
Manually annotated by BRENDA team
no activity in Trichaptum fusco-violaceum
white rot fungus
-
-
Manually annotated by BRENDA team
no activity in Trichaptum fusco-violaceum T21
white rot fungus
-
-
Manually annotated by BRENDA team
Pandorea sp.
-
-
-
Manually annotated by BRENDA team
strain T51, white rot fungus
-
-
Manually annotated by BRENDA team
strain T51, white rot fungus
-
-
Manually annotated by BRENDA team
virulent isolate B24 and hypovirulent isolate SS41
-
-
Manually annotated by BRENDA team
strain T7, white rot fungus
-
-
Manually annotated by BRENDA team
strain T7, white rot fungus
-
-
Manually annotated by BRENDA team
strain PRL572
-
-
Manually annotated by BRENDA team
isolated from pH-adjusted bleaching filtrates collected from mills producing mechanical pulp or kraft pulp, enzymes ODCs B, C, E, and F under mill-like conditions from selected filtrates B (pH 7.9), F (pH 7.4), H (pH 7.8), and I (pH 7.6)
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
oxalate decarboxylase belongs to the low-pH-inducible cupin superfamily of enzymes
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Oxalate
?
show the reaction diagram
Oxalate
Formate + CO2
show the reaction diagram
oxalate + H+
CO2 + formate
show the reaction diagram
oxalate + H+
formate + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Oxalate
?
show the reaction diagram
Oxalate
Formate + CO2
show the reaction diagram
oxalate + H+
formate + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O2
required for catalysis
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Biomimetic monochlorotriazinyl dyes
-
bearing a mercaptopyruvate at the terminal biomimetic moiety, competitive against oxalate
-
Chlorite
-
26% residual activity at 8.0 mM
Co2+
-
complete inhibition at 10 mM
Dithionite
formic acid
-
75% residual activity at 20 mM
glycolic acid
-
88% residual activity at 20 mM
hydrogen peroxide
-
5% residual activity at 20 mM
hydroxylamine
-
-
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
oxalate
substrate inhibition
phosphate
-
competitive
sulfite
-
complete inhibition at 1.0 mM
Surface-active ionic substances
-
anionic or cationic
-
additional information
-
up to 4 mM chlorate has no inhibitory effect on oxalate decarboxylase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 97
oxalate
5 - 7
oxalic acid
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 57
oxalate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 6.309
oxalate
185
11
oxalic acid
Bacillus subtilis
-
His-tagged recombinant enzyme; non-His-tagged recombinant enzyme
2093
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
nitric oxide
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apparent value, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.4
-
purified recombinant mutants R92K/R270K, E162Q and E333Q
0.7
-
purified recombinant mutant E162Q/E333Q
1.3
-
purified recombinant mutant R92K
2.4
-
purified recombinant mutant R270K
4
-
purified recombinant mutant E333D
4.5
-
mutant enzyme T165V, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
6.567
-
purified truncated AtuOXDC
9
-
induced specific activity by 5 mM oxalic acid
14
-
non-induced specific activity, growth without oxalic acid
15
-
induced specific activity by 5 mM oxalic acid
17.5 - 18.3
-
purified secreted recombinant enzyme, pH 4.0, 25C
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
30 - 72
-
purified wild-type enzyme, dependent on purification procedure
41
-
strain R/7, induced specific activity by 5 mM oxalic acid
48
-
mutant enzyme S161A, in 50 mM sodium acetate, pH 4.2, temperature not specified in the publication
65
pH 5, 26C, recombinant YvrK
86
-
induced specific activity by 5 mM oxalic acid
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
soluble and immobilized enzyme
4.2 - 5.7
-
assay at
additional information
-
pH-dependence of OxDC activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
3 - 5
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about 20% of maximal activity at pH 3.0 and 5.0
4.2 - 6.7
-
-
7.5
-
not active above
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21 - 22
-
assay at
22
-
assay at
23
-
assay at
45 - 65
50
-
soluble and immobilized enzyme
additional information
CO2 assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
-
the soluble enzyme shows at least more than 50% activity between 30 and 70C. The immobilized enzyme almost retains its full maximum activity at 70C (7% decrease of activity), while the soluble enzyme shows about 50% activity at 70C
additional information
-
1.7fold stimulation after incubation at 50C for 10 min, may be due to inactivation of heat labile proteases
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3
-
the enzyme has two pI-values of 2.3 and 3.0
2.5
-
the enzyme has two pI-values at 2.5 and 3.3
2.6
-
the enzyme has two pI-values at 2.6 and 4.2
3.3
-
the enzyme has two pI-values at 2.5 and 3.3
5.7
-
recombinant enzyme mutant T165V has two isoelectric points at pH 4.2 and pH 5.7
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43407
-
5 * 44000, SDS-PAGE, 5 * 43407, calculated from the amino acid sequence, pentamer, but it is possible, that YvrK is actually a hexamer
44700
-
estimated from amino acid sequence
48400
-
calculated from amino acid sequence
50000
x * 50000, deglycosylated form, calculated from the amino acid sequence
55000
-
x * 55000, enzyme decglycosylated by endo-beta-N-acetylglucosaminidase, SDS-PAGE
59000
-
x * 59000, SDS-PAGE
104000 - 110000
-
-
110000
-
deglycosylated protein
118000
220000
-
gel filtration
222000
recombinant YvrK, nondenaturing PAGE
254000
recombinant YvrK, gel filtration
560000
-
the high apparent MW obtained by gel filtration can be due to the tendency of certain glycoproteins to interact noncovalently in solution, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homohexamer
monomeric and hexameric structure
pentamer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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, 17C, 1 week, X-ray diffraction structure determination and analysis at 2.31 A resolution
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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, 17C, 2 months, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution
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purified recombinant mutants R92A, DELTA162-163, S161A, and E162A, hanging-drop vapour diffusion method at 18C, 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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
30
-
30 min, in presence of 10% SDS, retains 45% of its activity
60 - 70
-
both soluble and immobilized enzyme lose their activity continuously at 60C 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
60
-
30 min, in presence of 10% SDS, complete inactivation
80
-
20 min, 22% loss of activity
96
-
10 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
albumin, gelatin or surface-active non-ionic substances protect against thermal inactivation or denaturation by air
-
crystallization of OxDc noticeably increases the enzyme's specific activity and broadenes its pH-activity profile at both acidic pH 3.0 and neutral pH 7.0
-
O2 pressures higher than 0.04 atm of O2 accelerate the denaturation of the enzyme even in the presence of o-phenylenediamine
-
p-phenylenediamine, o-diphenols, p-diphenols and p-aromatic diamines protect against thermal inactivation or denaturation by air
-
retains 45% of its activity after incubation with 10% SDS for 30 min at room temperature. Almost complete loss of activity after 30 min, in presence of 10% SDS
-
under the condition of enzyme/support ratio at 1:20, pH 9, with 1.5 M (NH4)2SO4, 22C, 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
-20C, frozen in liquid nitrogen, pH buffered at or near 7, stable
-
0-3C, 0.2 M acetate buffer, pH 5.6, stable for several months
-
4C, 1 mg/ml protein, 0.02 M potassium acetate, more than 70% of the initial activity is retained after 4 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography, gel filtration
-
Ni-NTA resin chromatography
-
nickel affinity column chromatography
-
recombinant C-terminally His-tagged OxdC from Escherichia coli strain BL21(DE3)
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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 wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography
-
recombinant YvrK, 20.7fold
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Lactobacillus plantarum strain NC8
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expressed in Nicotiana tabacum
-
expression in Escherichia coli BL21(DE3)
-
expression of functionally inactive OXDC in Escherichia coli, expression of active OXDC in Nicotiana tabaccum var. Petite Havanna and tomato plants var. Pusa Ruby in cytosol and vacuole
gene FvOXDC, recombinant expression in Solanum lycopersicum fruits under the control of a fruit-specific promoter E8.2 being active upon ethylene induction only in ripening fruits, via Agrobacterium tumefaciens-mediated transformation, OXDC is targeted to the cell vacuole in the transgenic fruits. The transgenic fruits show up to a 90% reduction in oxalate content, which correlates with concomitant increases in calcium, iron, and citrate, compared to wild-type fruits. Expression of OXDC affects neither CO2 assimilation rates nor results in any detectable morphological differences in the transgenic plants. OXDC-responsive proteins involved in metabolism and stress responses represent the most substantially up- and down-regulated categories, respectively, in the transgenic fruit, compared with those of wild-type plants, proteome analysis, overview
-
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, DNA and amino acid sequence determination and analysis, expression of the enzyme in transgenic lettuce, Lactuca sativa cv. Veronica, plants using Agrobacterium tumefaciens strain EHA 105-mediated transformation
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 42C
-
recombinant expression of His6-tagged Mn(II)-substituted W132F enzyme mutant
-
transgenic overexpressionin Nicotiana tabacum plants. The transgenic plants contain less oxalic acid and more formic acid compared with the control plants and show enhanced resistance to cell death induced by exogenous oxalate and MpNEP2, a Nep1-like protein of the hemibiotrophic fungus Moniliophthora perniciosa. inhibition of reactive oxygen species formation in the transgenic plants inoculated with oxalate, MpNEP2, or a combination of both programmed cell death elicitors
-
yoaN gene, overexpression in Escherichia coli BL21(DE3)pLysS; yvrK gene, overexpression in Escherichia coli BL21(DE3)pLysS
yvrK gene, expression in Escherichia coli B834 (DE3)
yvrk gene, expression in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
OxDC expression is induced by addition of inorganic acids including hydrochloric acid, sulfuric acid, and phosphoric acid to culture media
YvrI is essential for acid stress induction of oxdC transcription, YvrI and YvrL regulate OxdC accumulation in response to acid stress
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D297A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
E101A
-
the mutant shows strongly decreased activity
E101D
-
the mutant shows strongly decreased activity
E101Q
-
the mutant shows strongly decreased activity
E101Q/E280Q
-
the mutant shows strongly decreased activity
E162A/N163S/S164N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E162Q/E333Q
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
E280A
-
the mutant shows strongly decreased activity
E280D
-
the mutant shows strongly decreased activity
E280Q
-
the mutant shows strongly decreased activity
E333D
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
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
R270E
mutant with 20fold reduced CO2 production
R270Q
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R92K/R270K
-
site-directed mutagenesis, the mutant enzyme shows altered kinetics and reduced activity compared to the wild-type enzyme
S161D/E162A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S161D/E162A/N163S
site-directed mutagenesis, almost inactive mutant
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
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
Y340F
mutant with 13fold reduced CO2 production
E162A
-
Mn2+-binding site 1 mutant, inactive
-
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
-
E333Q
-
Mn2+-binding site 2 mutant, inactive
-
R270K
-
Mn2+-binding site 2 mutant, kcat/Km is 43% that of wild-type
-
R92A
-
Mn2+-binding site 1 mutant, inactive
-
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
-
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
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
biotechnology
degradation
-
oxalic acid removal in industrial bleaching plant filtrates containing oxalic acid
industry
medicine
paper production
synthesis
-
biomimetic dyes may prove to be useful technological tools, suitable for the purification
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