Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Citrobacter braakii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
45000 | - |
x * 45000, SDS-PAGE | Citrobacter braakii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter braakii | Q8VQF6 | CinA, part of putative operon consisting of three open reading frames. CinB and cinC appear to encode the expected redox partners for a catalytically functional P450 system | - |
Purification (Comment) | Organism |
---|---|
- |
Citrobacter braakii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,8-cineole + [reduced flavodoxin] + O2 | enzyme displays a high affinity for cineole 1 with KD 0.7 microM, and a large spin state change of the heme iron associated with binding of cineole | Citrobacter braakii | (1R)-6beta-hydroxycineole + [oxidized flavodoxin] + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 45000, SDS-PAGE | Citrobacter braakii |
Synonyms | Comment | Organism |
---|---|---|
CYP176A | - |
Citrobacter braakii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | large spin state change of the heme iron associated with binding of cineole | Citrobacter braakii |