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1.14.15.1: camphor 5-monooxygenase

This is an abbreviated version!
For detailed information about camphor 5-monooxygenase, go to the full flat file.

Word Map on EC 1.14.15.1

Reaction

(+)-Camphor
+
reduced putidaredoxin
+
O2
=
(+)-exo-5-hydroxycamphor
+
oxidized putidaredoxin
+
H2O

Synonyms

2-bornanone 5-exo-hydroxylase, bornanone 5-exo-hydroxylase, CamC, camphor 5-exo-hydroxylase, camphor 5-exo-methylene hydroxylase, camphor 5-exohydroxylase, camphor 5-hydroxylase, Camphor 5-monooxygenase, camphor hydroxylase, camphor hydroxylase cytochrome P450cam, camphor methylene hydroxylase, camphor monooxygenase, class I cytochrome P450, CYP101, CYP101A1, CYP101B1, CYP101C1, CYP101D1, CYP101D2, CYP111A2, Cyt P450cam, cytochrome P-450-CAM, cytochrome P450 cam, cytochrome P450(cam), cytochrome p450cam, cytochrome P450cam monooxygenase, d-camphor monooxygenase, D-camphor-exo-hydroxylase, haem mono-oxygenase CYP101, methylene hydroxylase, methylene monooxygenase, moe, oxygenase, camphor 5-mono-, P450cam, P450cam monooxygenase, P450tcu

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.15.1 camphor 5-monooxygenase

Cofactor

Cofactor on EC 1.14.15.1 - camphor 5-monooxygenase

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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
-
state of cytochrome that is two equivalents of oxidation greater than the ferric form (Cpd I species), state of cytochrome that is one equivalent of oxidation greater than the ferric form (Cpd II species), two-electron-oxidized state of P450 or peroxidases containing both an oxoferryl center [FeIV=O] and either a tryptophanyl or tyrosyl radical, analogous to Cpd ES in cytochrome c peroxidase (Cpd ES species)
-
cytochrome b5
a cytochrome P450 enzyme, cytochrome b5 is bound in the reduced CYP101-camphor-carbon monoxide complex, cytochrome b5 perturbs many of the same resonances in the complex as Pdx, including those for residues involved in substrate access to and orientation within the active site of CYP101, chemical shifts, overview
-
cytochrome m
-
cytochrome P-450
-
-
cytochrome P450
-
FAD
-
increase of activity, can replace FMN
Ferredoxin
-
NADPH
putidaredoxin
-
additional information
catalytic turnover in P450cam requires the enzymes putidaredoxin (Pdx) and putidaredoxin reductase (Pdr), which mediate electron transfer from NADH to heme, the process is tightly coupled to substrate hydroxylation
-