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Literature summary extracted from

  • Eriksson, K.E.; Habu, N.; Samejima, M.
    Recent advances in fungal cellobiose oxidoreductases (1993), Enzyme Microb. Technol., 15, 1002-1008.
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.99.18 extracellular
-
 Phanerodontia chrysosporium
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.99.18 89170
-
 laser-induced desorption mass spectrometry Phanerodontia chrysosporium
1.1.99.18 93000
-
-
 Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.18 cellobiose + O2 Phanerodontia chrysosporium role in cellulose and probable in lignin degradation, physiologically significant electron acceptor may or may not be oxygen cellobiono-1,5-lactone + H2O2
-
 ?
1.1.99.18 cellobiose + O2 Phanerodontia chrysosporium K 3 role in cellulose and probable in lignin degradation, physiologically significant electron acceptor may or may not be oxygen cellobiono-1,5-lactone + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.18 Phanerodontia chrysosporium
-
-
-
1.1.99.18 Phanerodontia chrysosporium
-
 white-rot fungus
-
1.1.99.18 Phanerodontia chrysosporium
-
 earlier name: Sporotrichum pulverulentum
-
1.1.99.18 Phanerodontia chrysosporium K 3
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.1.99.18 glycoprotein carbohydrate content: 11.9% Phanerodontia chrysosporium
1.1.99.18 glycoprotein mannose is the predominant sugar Phanerodontia chrysosporium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.18 cellobiose + O2 molecular O2 as electron acceptor Phanerodontia chrysosporium cellobiono-1,5-lactone + H2O2
-
 ?
1.1.99.18 cellobiose + O2 role in cellulose and probable in lignin degradation, physiologically significant electron acceptor may or may not be oxygen Phanerodontia chrysosporium cellobiono-1,5-lactone + H2O2
-
 ?
1.1.99.18 cellobiose + O2 molecular O2 as electron acceptor Phanerodontia chrysosporium K 3 cellobiono-1,5-lactone + H2O2
-
 ?
1.1.99.18 cellobiose + O2 role in cellulose and probable in lignin degradation, physiologically significant electron acceptor may or may not be oxygen Phanerodontia chrysosporium K 3 cellobiono-1,5-lactone + H2O2
-
 ?
1.1.99.18 cellodextrin + O2 higher cellodextrins Phanerodontia chrysosporium aldonic acid + H2O2
-
 ?
1.1.99.18 cellodextrin + O2 higher cellodextrins Phanerodontia chrysosporium K 3 aldonic acid + H2O2
-
 ?
1.1.99.18 cellulose + O2 cellulose as electron donor, 10times lower oxidation rate than with cellobiose Phanerodontia chrysosporium ?
-
 ?
1.1.99.18 cellulose + O2 cellulose as electron donor, 10times lower oxidation rate than with cellobiose Phanerodontia chrysosporium K 3 ?
-
 ?
1.1.99.18 additional information enzyme reduces cytochrome c, 200 times faster than with oxygen, 2,6-dichlorophenolindophenol, phenoxy- and cation-radicals, a vatiety of quinones and Fe(III) compounds, the latter reduced 35-50 times faster than with oxygen, enzyme has a cellulose-binding domain Phanerodontia chrysosporium ?
-
 ?
1.1.99.18 additional information enzyme reduces cytochrome c, 200 times faster than with oxygen, 2,6-dichlorophenolindophenol, phenoxy- and cation-radicals, a vatiety of quinones and Fe(III) compounds, the latter reduced 35-50 times faster than with oxygen, enzyme has a cellulose-binding domain Phanerodontia chrysosporium K 3 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.99.18 monomer
-
 Phanerodontia chrysosporium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.99.18 0.4
-
 cellulose ferricyanide as electron acceptor Phanerodontia chrysosporium
1.1.99.18 3.6
-
 cellobiose ferricyanide as electron acceptor Phanerodontia chrysosporium

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.18 cytochrome b
-
 Phanerodontia chrysosporium
1.1.99.18 FAD FAD domain has all properties of cellobiose:quinone oxidoreductase, and could be formed by proteolytic cleavage of CBO into 55 kDa FAD and 35 kDd heme domain by papain, cellulose-binding site is located on the FAD domain Phanerodontia chrysosporium
1.1.99.18 heme b heme group: cytochrome b type, inactivated at higher pH levels, caused by conformational changes of protein, heme is necessary for reduction of cytochrome c, it acts as a single electron reductant, 35 kDa heme-containing domain Phanerodontia chrysosporium