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

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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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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
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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
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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
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034
(+)-Camphor
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pH 7.0, 32°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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more than 60% of maximum activity within
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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microsomal membrane
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Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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x * 58000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 58000, SDS-PAGE
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.161)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)