Literature summary extracted from
Hawkes, D.B.; Adams, G.W.; Burlingame, A.L.; Ortiz de Montellano, P.R.; De Voss, J.J.
Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization (2002), J. Biol. Chem., 277, 27725-27732.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.14.14.133 |
expression in Escherichia coli |
Citrobacter braakii |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.14.14.133 |
45000 |
- |
x * 45000, SDS-PAGE |
Citrobacter braakii |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.14.14.133 |
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 (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.14.14.133 |
- |
Citrobacter braakii |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.14.14.133 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
1.14.14.133 |
? |
x * 45000, SDS-PAGE |
Citrobacter braakii |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.14.14.133 |
CYP176A |
- |
Citrobacter braakii |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.14.14.133 |
heme |
large spin state change of the heme iron associated with binding of cineole |
Citrobacter braakii |
|