EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.99.18 | extracellular | - |
Phanerodontia chrysosporium | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.99.18 | Phanerodontia chrysosporium | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.99.18 | culture medium | - |
Phanerodontia chrysosporium | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.99.18 | cellobiose + ferricytochrome c | intact CBOR fully reduced with cellobiose, CBOR partially reduced by ascorbate and isolated ascorbate-reduced heme domain, all transfer electrons at similar rates to cytochrome c. Reduction of cationic one-electron acceptors via the heme group supports an electron transfer chain model | Phanerodontia chrysosporium | cellobiono-1,5-lactone + ferrocytochrome c | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.99.18 | CBOR | - |
Phanerodontia chrysosporium |
1.1.99.18 | cellobiose oxidoreductase | - |
Phanerodontia chrysosporium |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.99.18 | FAD | the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme | Phanerodontia chrysosporium | |
1.1.99.18 | heme | the heme domain is a one-electron reducing system | Phanerodontia chrysosporium | |
1.1.99.18 | protoheme | the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme | Phanerodontia chrysosporium |