Any feedback?
Information on EC 4.1.1.2 - oxalate decarboxylase
for references in articles please use BRENDA:EC4.1.1.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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 expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
oxalate decarboxylase, oxdc, oxazyme, oxdc-clec, fvoxdc, odc c, oxalate-decarboxylase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtuOXDC
Decarboxylase, oxalate
-
-
-
-
ODC
odc2
oxalate carboxy-lyase
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
OxDcase
pBy
YoaN
YvrK
additional information
AtuOXDC
-
putative recombinant enzyme, contains N- and C-cupin domains of OXDC
AtuOXDC
Agrobacterium tumefaciens C58 / ATCC 33970
-
putative recombinant enzyme, contains N- and C-cupin domains of OXDC
-
ODC
Atheliachaete sanguinea T51
-
-
-
ODC
no activity in Ceriporiopsis subvermispora CZ-3
-
-
-
ODC
no activity in Nematoloma frowardii b19
-
-
-
ODC
no activity in Phanerochaete chrysosporium F1767
-
-
-
ODC
no activity in Phlebiopsis gigantea T55
-
-
-
ODC
no activity in Radulodon erikssonii T84
-
-
-
ODC
no activity in Trichaptum fusco-violaceum T21
-
-
-
OXDC
-
-
OXDC
-
additional information
enzyme belongs to the cupin superfamily, bicupin
additional information
the enzyme is a member of the cupin superfamily of proteins
additional information
enzyme belongs to the cupin superfamily, bicupin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxalate = formate + CO2
catalytic mechanism of oxalate decarboxylase compared to oxalate oxidase, EC 1.2.3.4
oxalate = formate + CO2
catalytic mechanism, the N-terminal Mn-binding site can mediate catalysis involving the important residue Asp92
-
oxalate = formate + CO2
minimal, two step kinetic mechanism for enzyme-catalyzed decarboxylation proton-coupled electron transfer and decarboxylation
oxalate = formate + CO2
minimal, two step kinetic mechanism for enzyme-catalyzed decarboxylation proton-coupled electron transfer and decarboxylation
-
-
oxalate = formate + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9024-97-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Formate + CO2
-
-
traces of H2O2 and oxidation products of aromatic amines and phenols are formed, these aromatic compounds are added with the purpose of stimulating and protecting the enzyme during its catalytic action
?
Oxalate
Formate + CO2
-
the first two steps of the catalytic mechanism are reversible, the last step is irreversible
-
-
ir
oxalate + H+
formate + CO2
Atheliachaete sanguinea
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
Atheliachaete sanguinea T51
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
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
-
?
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-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
-
-
?
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
-
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
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
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
involved in the elevation of cytoplasmic pH
-
?
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
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
Bacillus subtilis 168 / CU1065
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
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
oxalate-catabolizing enzyme
-
?
oxalate + H+
formate + CO2
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
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
-
-
?
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
?
-
the enzyme also shows oxalate oxidase activity, catalytic cycle, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Atheliachaete sanguinea
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
Atheliachaete sanguinea T51
-
inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
-
?
oxalate + H+
formate + CO2
-
-
-
-
?
oxalate + H+
formate + CO2
involved in the elevation of cytoplasmic pH
-
?
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-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
-