Information on EC 1.14.13.161 - (+)-camphor 6-exo-hydroxylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.13.161
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RECOMMENDED NAME
GeneOntology No.
(+)-camphor 6-exo-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-camphor + NADPH + H+ + O2 = (+)-6-exo-hydroxycamphor + NADP+ + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(+)-camphor,NADPH:oxygen oxidoreductase (6-exo-hydroxylating)
A cytochrome P-450 monooxygenase isolated from Salvia officinalis (sage). Involved in the catabolism of camphor in senescent tissue.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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pathway for camphor degradation follows the oxidative ring opening sequence from (+)-camphor to 6-hydroxycamphor, 6-oxocamphor, alpha-campholonic acid, and 2-hydroxy-alpha-campholonic acid. The catabolism of camphor via 1,2-campholide is a minor degradative pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-camphor + NADPH + H+ + O2
(+)-6-exo-hydroxycamphor + NADP+ + H2O
show the reaction diagram
limonene + NADPH + H+ + O2
(-)-perillyl alcohol + NADP+ + H2O
show the reaction diagram
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additional information
?
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the microsomal camphor-6-exo-hydroxylase system requires molecular oxygen and a reduced pyridine nucleotide
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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enzyme is a cytochrome P450-dependent monooxygenase
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NADH
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21% of the rate with NADPH
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MnCl2
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upon treatment of sage suspension cultures with 30 mM MnCI2, camphor-6-hydroxylase activity is induced up to 7fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
clotrimazole
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84% inhibition at 0.05 mM
CO
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73% inhibition at CO:O2 ratio of 9:1, activity is partially restored by blue light
cytochrome c
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95% inhibition at 0.05 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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inclusion of both FAD and FMN in the incubation mixture enhances hydroxylation activity 2.4fold
FMN
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inclusion of both FAD and FMN in the incubation mixture enhances hydroxylation activity 2.4fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034
(+)-Camphor
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pH 7.0, 32°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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more than 60% of maximum activity within
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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microsomal membrane
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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x * 58000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 58000, SDS-PAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the genes responsible for early steps of D-camphor degradation, i.e. 5-exo-hydroxycamphor dehydrogenase, camD gene, cytochrome P-450cam, camC, NADH-putidaredoxin reductase camA, and putidaredoxin camB form an operon, camDCAB, and are under negative control by the gene camR located immediately upstream from the camD gene
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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functional expression in Escherichia coli of tricistronic constructs consisting of P450cam and the auxiliary proteins, Pd and PdR. Transformed bacterial whole cells efficiently oxidize (1R)-(+)-camphor to 6-exo-hydroxycamphor and interestingly limonene to (-)-perillyl alcohol. These bioengineered Escherichia coli cells possess a heterologous selfsufficient P450 catalytic system