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

BRENDA support

Literature summary extracted from

  • Mason, M.G.; Nicholls, P.; Divne, C.; Hallberg, B.M.; Henriksson, G.; Wilson, M.T.
    The heme domain of cellobiose oxidoreductase: a one-electron reducing system (2003), Biochim. Biophys. Acta, 1604, 47-54.
    View publication on PubMed

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.18 Phanerodontia chrysosporium
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.99.18 culture medium
-
 Phanerodontia chrysosporium
-

Substrates and Products (Substrate)

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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.99.18 CBOR
-
 Phanerodontia chrysosporium
1.1.99.18 cellobiose oxidoreductase
-
 Phanerodontia chrysosporium

Cofactor

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