1.14.14.133: 1,8-cineole 2-endo-monooxygenase
This is an abbreviated version!
For detailed information about 1,8-cineole 2-endo-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.133
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1.14.14.133
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p450cam
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heme
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monooxygenases
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h-bonding
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citrobacter
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monoterpenes
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fmn
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substrate-bound
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fmn-containing
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braakii
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substrate-free
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monoterpenoid
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sesquiterpene
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s-oxidations
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bicyclic
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terpene
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ferryl
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low-spin
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regioselective
- 1.14.14.133
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p450cam
- heme
- monooxygenases
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h-bonding
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citrobacter
- monoterpenes
- fmn
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substrate-bound
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fmn-containing
- braakii
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substrate-free
-
monoterpenoid
-
sesquiterpene
-
s-oxidations
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bicyclic
-
terpene
-
ferryl
-
low-spin
-
regioselective
Reaction
Synonyms
CinA, CYP176A, CYP176A1, EC 1.14.13.156, P450cin
ECTree
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Cofactor
Cofactor on EC 1.14.14.133 - 1,8-cineole 2-endo-monooxygenase
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NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
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redox partner is cindoxin, containing FMN. Cindoxin might be different to other flavodoxins that interact with P450s, as both redox states of cindoxin could be catalytically relevant. Cindoxin supports regio- and stereoselective P450cin-catalysed cineole oxidation to (1R)-6beta-hydroxycineole with turnover rates up to 1500 per min
FMN
the FAD/FMN reductase consists of two separate polypeptides where the FMN protein, cindoxin, shuttles electrons between the FAD-containing cindoxin reductase and P450cin. Reaction is highly ionic strength-dependent. The fully reduced hydroquinone is the electron-donating species. Surface interactions are rather different from other P450 proteins
large spin state change of the heme iron associated with binding of cineole