Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Maekelae, M.R.; Hilden, K.; Lundell, T.K.
    Oxalate decarboxylase: biotechnological update and prevalence of the enzyme in filamentous fungi (2010), Appl. Microbiol. Biotechnol., 87, 801-814.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.1.2 agriculture control of fungal plant pathogen Pandorea sp.
4.1.1.2 biotechnology determination of oxalic acid in food and biological samples like urine, plasma, serum, wort and beer Flammulina velutipes
4.1.1.2 biotechnology determination of oxalic acid in food and biological samples like urine, plasma, serum, wort and beer Flammulina sp.
4.1.1.2 industry prevention of scaling in pulp and paper industry, depletion of oxalate from beverage Aspergillus niger
4.1.1.2 industry prevention of scaling in pulp and paper industry, depletion of oxalate from beverage Aspergillus sp.
4.1.1.2 medicine treatment of hyperoxaluria, urolithiasis, nephrocalcinosis, and depletion of dietary oxalate with enzyme formulation Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ required for catalysis Bacillus subtilis
4.1.1.2 Mn2+ required for catalysis Aspergillus niger
4.1.1.2 Mn2+ required for catalysis Agaricus bisporus
4.1.1.2 Mn2+ required for catalysis Trametes versicolor
4.1.1.2 Mn2+ required for catalysis Flammulina velutipes
4.1.1.2 Mn2+ required for catalysis Aspergillus sp.
4.1.1.2 Mn2+ required for catalysis Phanerodontia chrysosporium
4.1.1.2 Mn2+ required for catalysis Dichomitus squalens
4.1.1.2 Mn2+ required for catalysis Flammulina sp.
4.1.1.2 Mn2+ required for catalysis Pandorea sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.2 104000
-
-
 Phanerodontia chrysosporium
4.1.1.2 104000 110000
-
 Dichomitus squalens
4.1.1.2 110000
-
 deglycosylated protein Agaricus bisporus
4.1.1.2 118000
-
-
 Trametes versicolor
4.1.1.2 118000
-
 glycosylated protein Agaricus bisporus
4.1.1.2 128000
-
-
 Flammulina velutipes

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.2 oxalate + H+ Bacillus subtilis
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Aspergillus niger
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Agaricus bisporus
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Trametes versicolor
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Flammulina velutipes
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Aspergillus sp.
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Phanerodontia chrysosporium
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Dichomitus squalens
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Flammulina sp.
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Pandorea sp.
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Pandorea sp. OXJ-11a
-
 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Flammulina sp. IJF 140502
-
 formate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Agaricus bisporus
-
-
-
4.1.1.2 Aspergillus niger
-
-
-
4.1.1.2 Aspergillus sp.
-
-
-
4.1.1.2 Bacillus subtilis
-
-
-
4.1.1.2 Dichomitus squalens
-
-
-
4.1.1.2 Flammulina sp.
-
-
-
4.1.1.2 Flammulina sp. IJF 140502
-
-
-
4.1.1.2 Flammulina velutipes
-
-
-
4.1.1.2 Pandorea sp.
-
-
-
4.1.1.2 Pandorea sp. OXJ-11a
-
-
-
4.1.1.2 Phanerodontia chrysosporium
-
-
-
4.1.1.2 Trametes versicolor
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.2 glycoprotein
-
 Agaricus bisporus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 oxalate + H+
-
 Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Aspergillus niger formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Agaricus bisporus formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Trametes versicolor formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Flammulina velutipes formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Aspergillus sp. formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Phanerodontia chrysosporium formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Dichomitus squalens formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Flammulina sp. formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Pandorea sp. formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Pandorea sp. OXJ-11a formate + CO2
-
 ?
4.1.1.2 oxalate + H+
-
 Flammulina sp. IJF 140502 formate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Bacillus subtilis
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Aspergillus niger
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Agaricus bisporus
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Trametes versicolor
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Flammulina velutipes
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Aspergillus sp.
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Phanerodontia chrysosporium
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Dichomitus squalens
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Flammulina sp.
4.1.1.2 hexamer functional ODC enzyme is a hexamer comprised of two trimers of the bicupin subunits Pandorea sp.

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 ODC
-
 Bacillus subtilis
4.1.1.2 ODC
-
 Aspergillus niger
4.1.1.2 ODC
-
 Agaricus bisporus
4.1.1.2 ODC
-
 Trametes versicolor
4.1.1.2 ODC
-
 Flammulina velutipes
4.1.1.2 ODC
-
 Aspergillus sp.
4.1.1.2 ODC
-
 Phanerodontia chrysosporium
4.1.1.2 ODC
-
 Dichomitus squalens
4.1.1.2 ODC
-
 Flammulina sp.
4.1.1.2 ODC
-
 Pandorea sp.
4.1.1.2 oxalate carboxy-lyase
-
 Bacillus subtilis
4.1.1.2 oxalate carboxy-lyase
-
 Aspergillus niger
4.1.1.2 oxalate carboxy-lyase
-
 Agaricus bisporus
4.1.1.2 oxalate carboxy-lyase
-
 Trametes versicolor
4.1.1.2 oxalate carboxy-lyase
-
 Flammulina velutipes
4.1.1.2 oxalate carboxy-lyase
-
 Aspergillus sp.
4.1.1.2 oxalate carboxy-lyase
-
 Phanerodontia chrysosporium
4.1.1.2 oxalate carboxy-lyase
-
 Dichomitus squalens
4.1.1.2 oxalate carboxy-lyase
-
 Flammulina sp.
4.1.1.2 oxalate carboxy-lyase
-
 Pandorea sp.
4.1.1.2 OXDC
-
 Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.2 O2 required for catalysis Bacillus subtilis
4.1.1.2 O2 required for catalysis Aspergillus niger
4.1.1.2 O2 required for catalysis Agaricus bisporus
4.1.1.2 O2 required for catalysis Trametes versicolor
4.1.1.2 O2 required for catalysis Flammulina velutipes
4.1.1.2 O2 required for catalysis Aspergillus sp.
4.1.1.2 O2 required for catalysis Phanerodontia chrysosporium
4.1.1.2 O2 required for catalysis Dichomitus squalens
4.1.1.2 O2 required for catalysis Flammulina sp.
4.1.1.2 O2 required for catalysis Pandorea sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.1.1.2 Trametes versicolor the enzyme has two pI-values of 2.3 and 3.0
-
 2.3
4.1.1.2 Flammulina velutipes the enzyme has two pI-values at 2.5 and 3.3
-
 2.5
4.1.1.2 Dichomitus squalens the enzyme has two pI-values at 2.6 and 4.2
-
 2.6
4.1.1.2 Agaricus bisporus the enzyme has two pI-values at 3.0 and 3.4
-
 3
4.1.1.2 Trametes versicolor the enzyme has two pI-values of 2.3 and 3.0
-
 3
4.1.1.2 Flammulina velutipes the enzyme has two pI-values at 2.5 and 3.3
-
 3.3
4.1.1.2 Agaricus bisporus the enzyme has two pI-values at 3.0 and 3.4
-
 3.4
4.1.1.2 Dichomitus squalens the enzyme has two pI-values at 2.6 and 4.2
-
 4.2