4.1.1.2: oxalate decarboxylase
This is an abbreviated version!
For detailed information about oxalate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.2
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4.1.1.2
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hyperoxaluria
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velutipes
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oxalate-degrading
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flammulina
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mniii
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mn-dependent
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bicupins
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collybia
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medicine
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agriculture
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paper production
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industry
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biotechnology
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degradation
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synthesis
- 4.1.1.2
- hyperoxaluria
- velutipes
-
oxalate-degrading
-
flammulina
-
mniii
-
mn-dependent
-
bicupins
-
collybia
- medicine
- agriculture
- paper production
- industry
- biotechnology
- degradation
- synthesis
Reaction
Synonyms
AnODC, AtuOXDC, Decarboxylase, oxalate, FvOXDC, More, ODC, ODC B, ODC C, ODC E, ODC F, odc2, oxalate carboxy-lyase, oxalate-decarboxylase, oxazyme, OXD, OXDC, OxDc-CLEC, OxDcase, OxdD, pBy, TOXDC, YoaN, YvrK
ECTree
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Substrates Products
Substrates Products on EC 4.1.1.2 - oxalate decarboxylase
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REACTION DIAGRAM
Formate + CO2
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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
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the first two steps of the catalytic mechanism are reversible, the last step is irreversible
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ir
oxalate + H+
formate + CO2
Atheliachaete sanguinea
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inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
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?
oxalate + H+
formate + CO2
Atheliachaete sanguinea T51
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inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae
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?
oxalate + H+
formate + CO2
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678138, 687082, 691955, 692903, 694237, 713879, 714726, 715299, 716726, 727124, 727707, 728195, 748313, 748822
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-
?
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
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?
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
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?
oxalate + H+
formate + CO2
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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
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?
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
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?
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
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?
oxalate + H+
formate + CO2
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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
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?
oxalate + H+
formate + CO2
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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
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?
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
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ir
oxalate + H+
formate + CO2
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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
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-
?
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
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?
oxalate + H+
formate + CO2
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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
-
?
?
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enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations
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?
additional information
?
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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
?
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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
?
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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
?
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the enzyme also shows oxalate oxidase activity, catalytic cycle, overview
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?
additional information
?
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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
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-
?