Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Phanerodontia chrysosporium | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture medium | - |
Phanerodontia chrysosporium | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CBOR | - |
Phanerodontia chrysosporium |
cellobiose oxidoreductase | - |
Phanerodontia chrysosporium |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme | Phanerodontia chrysosporium | |
heme | the heme domain is a one-electron reducing system | Phanerodontia chrysosporium | |
protoheme | the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme | Phanerodontia chrysosporium |