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Literature summary for 1.1.99.18 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
Search for more literature for 1.1.99.18

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Phanerodontia chrysosporium
-
-

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
 Phanerodontia chrysosporium
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
CBOR
-
 Phanerodontia chrysosporium
cellobiose oxidoreductase
-
 Phanerodontia chrysosporium

Cofactor

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