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Information on EC 1.2.7.10 - oxalate oxidoreductase and Organism(s) Moorella thermoacetica and UniProt Accession Q2RI41

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IUBMB Comments
Contains thiamine diphosphate and [4Fe-4S] clusters. Acceptors include ferredoxin and the nickel-dependent carbon monoxide dehydrogenase (EC 1.2.7.4)
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This record set is specific for:
Moorella thermoacetica
UNIPROT: Q2RI41
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The taxonomic range for the selected organisms is: Moorella thermoacetica
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
oxalate oxidoreductase, oxalate:ferredoxin oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Moth_1591
gene name, subunit beta
Moth_1592
gene name, subunit alpha
Moth_1593
gene name, subunit delta
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
oxalate:ferredoxin oxidoreductase
Contains thiamine diphosphate and [4Fe-4S] clusters. Acceptors include ferredoxin and the nickel-dependent carbon monoxide dehydrogenase (EC 1.2.7.4)
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
ir
2-oxobutyrate + methyl viologen
?
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + H2O + methyl viologen
?
show the reaction diagram
-
-
-
-
?
2-oxovalerate + H2O + methyl viologen
?
show the reaction diagram
-
very low activity
-
-
?
glyoxylate + methyl viologen
?
show the reaction diagram
-
-
-
-
?
oxalate + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
oxalate + cytochrome c
CO2 + reduced cytochrome c
show the reaction diagram
-
cytochrome c is the best electron acceptor
-
-
?
oxalate + FAD
CO2 + FADH2
show the reaction diagram
-
-
-
-
?
oxalate + ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
-
oxalate is the best substrate
-
-
?
oxalate + FMN
CO2 + FMNH2
show the reaction diagram
-
-
-
-
?
oxalate + methyl viologen
2 CO2 + reduced methyl viologen
show the reaction diagram
-
-
-
?
oxalate + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
oxalate + metronidazole
CO2 + reduced metronidazole
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O + methyl viologen
?
show the reaction diagram
-
-
-
-
?
pyruvate + methyl viologen
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
4Fe-4S-center
-
the enzyme contains three [Fe4S4] clusters
thiamine diphosphate
-
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
the enzyme contains 14 mol iron per mol protein
Mg2+
-
the enzyme contains 0.8 mol Mg2+ per mol protein
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
addition of CoA, acetyl-CoA, or succinyl-CoA to the assay has a minimal effect on the oxalate-dependent reduction of benzyl viologen
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058
oxalate
-
in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
oxalate
-
in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
-
enzyme from glucose-grown cells, at pH 7.9 and 55°C
0.4
-
enzyme from oxalate-grown cells, at pH 7.9 and 55°C
0.6
-
using benzyl viologen as a cosubstrate, in 50 mM Tris-HCl (pH 8.5), at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CoA has no effect on catalysis by OOR. OOR binds pyruvate and catalyzes decarboxylation to form the same hydroxyethylidine-thiamine diphosphate intermediate and one-electron transfer to generate the hydroxyethylidine-thiamine diphosphate radical as does pyruvate:ferredoxin oxidoreductase, EC 1.2.7.1. In OOR, this intermediate remains stranded at the active site as a covalent inhibitor. OOR generates an oxalate-derived adduct with thiamine diphosphate (oxalyl-TPP) that undergoes decarboxylation and one-electron transfer to form a radical intermediate remaining bound to thiamine diphosphate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
226900
-
analytical ultracentrifugation
236000
-
gel filtration
243000
-
native PAGE
32000
-
1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
33900
-
1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence
34200
-
1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence
36000
-
1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
43000
-
1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
43700
-
1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 8-11% (w/v) PEG 3000 and 3-4% (w/v) Tacsimate (pH 7.0)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, red agarose column chromatography, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daniel, S.; Pilsl, C.; Drake, H.
Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica
FEMS Microbiol. Lett.
231
39-43
2004
Moorella thermoacetica
Manually annotated by BRENDA team
Pierce, E.; Becker, D.F.; Ragsdale, S.W.
Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate
J. Biol. Chem.
285
40515-40524
2010
Moorella thermoacetica
Manually annotated by BRENDA team
Gibson, M.I.; Brignole, E.J.; Pierce, E.; Can, M.; Ragsdale, S.W.; Drennan, C.L.
The structure of an oxalate oxidoreductase provides insight into microbial 2-oxoacid metabolism
Biochemistry
54
4112-4120
2015
Moorella thermoacetica (Q2RI41)
Manually annotated by BRENDA team
Pierce, E.; Mansoorabadi, S.O.; Can, M.; Reed, G.H.; Ragsdale, S.W.
Properties of intermediates in the catalytic cycle of oxalate oxidoreductase and its suicide inactivation by pyruvate
Biochemistry
56
2824-2835
2017
Moorella thermoacetica (Q2RI41 and Q2RI42 and Q2RI40)
Manually annotated by BRENDA team