Literature summary for 1.14.14.133 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Citrobacter braakii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
45000	-	x * 45000, SDS-PAGE	Citrobacter braakii

Organism

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 (Commentary)

Purification (Comment)	Organism
-	Citrobacter braakii

Substrates and Products (Substrate)

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

Subunits	Comment	Organism
?	x * 45000, SDS-PAGE	Citrobacter braakii

Synonyms

Synonyms	Comment	Organism
CYP176A	-	Citrobacter braakii

Cofactor

Cofactor	Comment	Organism	Structure
heme	large spin state change of the heme iron associated with binding of cineole	Citrobacter braakii

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Release 2023.1 (January 2023)