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EC Tree
The taxonomic range for the selected organisms is: Oxalobacter formigenes The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
oxalyl-coa decarboxylase, oxalyl-coenzyme a decarboxylase, oxalyl coa decarboxylase, oxalyl coenzyme a decarboxylase,
more
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Oxalyl coenzyme A decarboxylase
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Decarboxylase, oxalyl coenzyme A
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Oxalyl coenzyme A decarboxylase
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oxalyl-coenzyme A decarboxylase
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OXC
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-
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oxalyl-CoA carboxy-lyase (formyl-CoA-forming)
A thiamine-diphosphate protein.
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Oxalyl-CoA
Formyl-CoA + CO2
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-
-
?
Oxalyl-CoA
Formyl-CoA + CO2
Oxalyl-CoA
Formyl-CoA + CO2
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-
-
-
?
Oxalyl-CoA
Formyl-CoA + CO2
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-
-
?
Oxalyl-CoA
Formyl-CoA + CO2
-
essential step in ATP generation
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-
?
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Oxalyl-CoA
Formyl-CoA + CO2
Oxalyl-CoA
Formyl-CoA + CO2
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-
-
-
?
Oxalyl-CoA
Formyl-CoA + CO2
-
essential step in ATP generation
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-
?
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thiamine diphosphate
required
thiamine diphosphate
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thiamine diphosphate
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required
thiamine diphosphate
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dependent on
thiamine diphosphate
dependent on
thiamine diphosphate
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Km: 1.1 picomol
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3-deazathiamine diphosphate
efficient inhibitor
CoA
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mixed inhibitor with respect to oxalyl-CoA
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0.018
oxalyl-CoA
mutant enzyme E121Q, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.021
oxalyl-CoA
mutant enzyme S553A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.0235
oxalyl-CoA
wild type enzyme
0.024
oxalyl-CoA
mutant enzyme Y483A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.04
oxalyl-CoA
mutant enzyme Y483F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.041
oxalyl-CoA
mutant enzyme E121A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.043
oxalyl-CoA
mutant enzyme Y120F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.06
oxalyl-CoA
mutant enzyme Y120A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.066
oxalyl-CoA
mutant enzyme R555A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.023
oxalyl-CoA
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pH 6.7, 30°C
0.0343
oxalyl-CoA
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at 37°C
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88
oxalyl-CoA
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pH 6.7, 30°C
0.1
oxalyl-CoA
mutant enzyme E121A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
0.26
oxalyl-CoA
mutant enzyme Y120A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
1.4
oxalyl-CoA
mutant enzyme Y483A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
1.7
oxalyl-CoA
mutant enzyme Y483F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
3.3
oxalyl-CoA
mutant enzyme E121Q, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
7.2
oxalyl-CoA
mutant enzyme Y120F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
13
oxalyl-CoA
mutant enzyme S553A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
85
oxalyl-CoA
mutant enzyme R555A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
88
oxalyl-CoA
wild type enzyme, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl
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Uniprot
brenda
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physiological function
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the commensal bacterium Oxalobacter formigenes consumes oxalate by converting it to oxalyl-CoA, which is decarboxylated by oxalyl-CoA decarboxylase
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OXC_OXAFO
568
0
60684
Swiss-Prot
-
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65000
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4 * 65000, SDS-PAGE
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tetramer
x-ray crystallography
tetramer
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tetramer
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4 * 65000, SDS-PAGE
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cocrystallization of wild-type OXC with 1 mM CoA, with a precipitating solution containing 0.5 M CaCl2, 0.1 M BisTris propane (2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl) propane-1,3-diol), pH 6.5, and 26% polyethylene glycol 550 monomethyl ether
recombinant, hanging drop vapour-diffusion method, native and seleno-methionine labelled enzyme is crystallized in two different conditions resulting in two different crystal forms, one showing poor diffraction and the other merohedral twinning. Crystals in the former category belong to the tetragonal space group P4(2)2(1)2, crystals in the latter category are obtained by cocrystallization of the protein with coenzyme A, thiamine diphosphate and Mg2+. The crystal is heavily twinned with a twin ratio of 0.43
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recombinant, hanging-drop vapour-diffusion method
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E121A
0.1% activity compared to the wild type enzyme
E121Q
3.8% activity compared to the wild type enzyme
E56A
no activity, mutant elutes with a retention time corresponding to that of a dimer
R555A
96% activity compared to the wild type enzyme
S553A
15% activity compared to the wild type enzyme
Y120A
0.3% activity compared to the wild type enzyme
Y120F
8.2% activity compared to the wild type enzyme
Y483A
1.6% activity compared to the wild type enzyme
Y483F
1.9% activity compared to the wild type enzyme
additional information
deletion mutant DELTA553-565 shows almost no activity
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Blue-sepharose column chromatography
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expressed in Escherichia coli
expressed in Escherichia coli
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expression in Escherichia coli
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medicine
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gene transfer to human cells for urolithiasis therapy, considered
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Baetz, A.L.; Allison, M.J.
Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes
J. Bacteriol.
171
2605-2608
1989
Oxalobacter formigenes
brenda
Lung, H.Y.; Cornelius, J.G.; Peck, A.B.
Cloning and expression of the Oxalyl-CoA decarboxylase gene from the bacterium, Oxalobacter formigenes: Prospects for gene therapy to control Ca-Oxalate kidney stone formation
Am. J. Kidney Dis.
17
381-385
1991
Oxalobacter formigenes
brenda
Lung, H.Y.; Baetz, A.L.; Peck, A.B.
Molecular cloning, DNA sequence, and gene expression of the oxalyl-coenzyme A decarboxylase gene, oxc, from the bacterium Oxalobacter formigenes
J. Bacteriol.
176
2468-2472
1994
Oxalobacter formigenes
brenda
Berthold, C.L.; Sidhu, H.; Ricagno, S.; Richards, N.G.; Lindqvist, Y.
Detection and characterization of merohedral twinning in crystals of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes
Biochim. Biophys. Acta
1764
122-128
2006
Oxalobacter formigenes
brenda
Berthold, C.L.; Moussatche, P.; Richards, N.G.; Lindqvist, Y.
Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate
J. Biol. Chem.
280
41645-41654
2005
Oxalobacter formigenes
brenda
Bendazzoli, C.; Turroni, S.; Gotti, R.; Olmo, S.; Brigidi, P.; Cavrini, V.
Determination of oxalyl-coenzyme A decarboxylase activity in Oxalobacter formigenes and Lactobacillus acidophilus by capillary electrophoresis
J. Chromatogr. B
854
350-356
2007
Lactobacillus acidophilus, Lactobacillus acidophilus LA 14, Oxalobacter formigenes
brenda
Berthold, C.L.; Toyota, C.G.; Moussatche, P.; Wood, M.D.; Leeper, F.; Richards, N.G.; Lindqvist, Y.
Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases
Structure
15
853-861
2007
Oxalobacter formigenes (P40149)
brenda
Abratt, V.R.; Reid, S.J.
Oxalate-degrading bacteria of the human gut as probiotics in the management of kidney stone disease
Adv. Appl. Microbiol.
72
63-87
2010
Bifidobacterium animalis subsp. lactis, Bifidobacterium dentium, Bifidobacterium dentium ATCC 27678, Bifidobacterium gallicum (D1NS77), Bifidobacterium gallicum DSM 20093 (D1NS77), Bradyrhizobium japonicum ORS278 (A4YXN1), Bradyrhizobium sp. (A4YXN1), Eggerthella lenta, Enterococcus faecalis, Escherichia coli, Escherichia coli ATCC 8739, Lactobacillus acidophilus (A4PE17), Lactobacillus acidophilus ATCC 4796 (A4PE17), Lactobacillus gasseri, Lactobacillus gasseri Gasser AM63, Lactobacillus johnsonii (C2E3B5), Lactobacillus johnsonii ATCC 33200 (C2E3B5), Limosilactobacillus reuteri, Limosilactobacillus reuteri 100-23, Oxalobacter formigenes (C3XBB9), Oxalobacter formigenes, Oxalobacter formigenes OXCC13 (C3XBB9), Paraburkholderia phytofirmans (B2T9D2), Paraburkholderia phytofirmans PsJN (B2T9D2), Providencia rettgeri (D4C4C5), Providencia rettgeri DSM 1131 (D4C4C5), Shigella boydii (Q31Y98), Shigella boydii Sb 227 (Q31Y98)
brenda
Mullins, E.A.; Sullivan, K.L.; Kappock, T.J.
Function and X-ray crystal structure of Escherichia coli YfdE
PLoS ONE
8
e67901
2013
Escherichia coli, Oxalobacter formigenes
brenda