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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.
    View publication on PubMed

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