4.1.1.2 additional information enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations Bacillus subtilis ? - ? 89 4.1.1.2 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 Bacillus subtilis ? - ? 89 4.1.1.2 additional information the enzyme also shows oxalate oxidase activity, catalytic cycle, overview Bacillus subtilis ? - ? 89 4.1.1.2 additional information enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations Bacillus subtilis 168 ? - ? 89 4.1.1.2 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 Bacillus subtilis 168 ? - ? 89 4.1.1.2 additional information the enzyme also shows oxalate oxidase activity, catalytic cycle, overview Bacillus subtilis 168 ? - ? 89 4.1.1.2 Oxalate - Cavia porcellus Formate + CO2 - ? 1347 4.1.1.2 Oxalate - Bacillus subtilis Formate + CO2 - ? 1347 4.1.1.2 Oxalate - Bacillus subtilis Formate + CO2 - ir 1347 4.1.1.2 Oxalate - Sclerotinia sclerotiorum Formate + CO2 - ? 1347 4.1.1.2 Oxalate - Aspergillus phoenicis Formate + CO2 - ? 1347 4.1.1.2 Oxalate - Trametes versicolor Formate + CO2 - ? 1347 4.1.1.2 Oxalate - Flammulina velutipes Formate + CO2 - ? 1347 4.1.1.2 Oxalate - Aspergillus niger 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 ? 1347 4.1.1.2 Oxalate the first two steps of the catalytic mechanism are reversible, the last step is irreversible Bacillus subtilis Formate + CO2 - ir 1347 4.1.1.2 Oxalate induction by oxalate Trametes versicolor ? - ? 369380 4.1.1.2 Oxalate induction by oxalate Flammulina velutipes ? - ? 369380 4.1.1.2 Oxalate induced by oxalate or succinate Sclerotinia sclerotiorum ? - ? 369380 4.1.1.2 oxalate + H+ - Lactiplantibacillus plantarum formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis formate + CO2 - ir 367893 4.1.1.2 oxalate + H+ - Mus musculus formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Aspergillus niger formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Agaricus bisporus formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Agrobacterium tumefaciens formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Sclerotinia sclerotiorum formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Trametes versicolor formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Flammulina velutipes formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Aspergillus sp. formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Phanerodontia chrysosporium formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Thermotoga maritima formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Dichomitus squalens formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Trametes ochracea formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Atheliachaete sanguinea formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Flammulina sp. formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Pandorea sp. formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - uncultured fungus formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ acts exclusively on oxalate Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ contains two potential active sites per subunit Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ enzyme structure, YvrK possesses two potential active sites per subunit, but only one could be fully occupied by manganese, mechanism, catalytic cycle Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ specific for oxalate Flammulina velutipes formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Trametes versicolor formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Dichomitus squalens formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Trametes ochracea formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Atheliachaete sanguinea formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ involved in the elevation of cytoplasmic pH Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ oxalate-catabolizing enzyme Flammulina velutipes formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ oxalate-degrading enzyme Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ir 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis 128 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ acts exclusively on oxalate Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ contains two potential active sites per subunit Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ enzyme structure, YvrK possesses two potential active sites per subunit, but only one could be fully occupied by manganese, mechanism, catalytic cycle Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ involved in the elevation of cytoplasmic pH Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis 168 formate + CO2 - ir 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis 168 formate + CO2 - ir 367893 4.1.1.2 oxalate + H+ oxalate-degrading enzyme Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton Bacillus subtilis 168 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis 168 / CU1065 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ 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 Bacillus subtilis 168 / CU1065 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Trametes ochracea T7 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Trametes ochracea T7 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Atheliachaete sanguinea T51 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Atheliachaete sanguinea T51 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis FNCC 0059 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Lactiplantibacillus plantarum KSK-II formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Pandorea sp. OXJ-11a formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Sclerotinia sclerotiorum 1980 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Flammulina sp. IJF 140502 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Agrobacterium tumefaciens C58 / ATCC 33970 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Dichomitus squalens PO114 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ inducible enzyme, key role in regulating the level of oxalate concentrations inside the fungal cells and in the vicinity of the fungal hyphae Dichomitus squalens PO114 formate + CO2 - ? 367893 4.1.1.2 oxalate + H+ - Bacillus subtilis CO2 + formate - ? 410019 4.1.1.2 oxalate + H+ - Aspergillus niger CO2 + formate - ? 410019 4.1.1.2 oxalate + H+ - Trametes versicolor CO2 + formate - ? 410019 4.1.1.2 oxalate + H+ - Bacillus subtilis 168 / CU1065 CO2 + formate - ? 410019 4.1.1.2 oxalate + H+ - Trametes versicolor PRL572 CO2 + formate - ? 410019