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EC Tree
IUBMB Comments A cytochrome P-450 monooxygenase isolated from Salvia officinalis (sage). Involved in the catabolism of camphor in senescent tissue.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
(+)-camphor 6-hydroxylase, P450cam,
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(+)-camphor 6-hydroxylase
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(+)-camphor + NADPH + H+ + O2 = (+)-6-exo-hydroxycamphor + NADP+ + H2O
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(+)-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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(+)-camphor + NADPH + H+ + O2
(+)-6-exo-hydroxycamphor + NADP+ + H2O
limonene + NADPH + H+ + O2
(-)-perillyl alcohol + NADP+ + H2O
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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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(+)-camphor + NADPH + H+ + O2
(+)-6-exo-hydroxycamphor + NADP+ + H2O
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(+)-camphor + NADPH + H+ + O2
(+)-6-exo-hydroxycamphor + NADP+ + H2O
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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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NADPH
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absolute requirement for NADPH and O2
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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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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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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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0.034
(+)-Camphor
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pH 7.0, 32°C
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6.5 - 7.5
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more than 60% of maximum activity within
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brenda
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brenda
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brenda
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microsomal membrane
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brenda
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microsomal membrane
brenda
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light membrane fraction
brenda
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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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58000
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x * 58000, SDS-PAGE
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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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expression in Escherichia coli
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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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Kim, D.; Ortiz de Montellano, P.R.
Tricistronic overexpression of cytochrome P450cam, putidaredoxin, and putidaredoxin reductase provides a useful cell-based catalytic system
Biotechnol. Lett.
31
1427-1431
2009
Pseudomonas putida
brenda
Funk, C.; Koepp, A.E.; Croteau, R.
Catabolism of camphor in tissue cultures and leaf disks of common sage (Salvia officinalis)
Arch. Biochem. Biophys.
294
306-313
1992
Salvia officinalis
brenda
Koga, H.; Yamaguchi, E.; Matsunaga, K.; Aramaki, H.; Horiuchi, T.
Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida
J. Biochem.
106
831-836
1989
Pseudomonas putida
brenda
Funk, C.; Croteau, R.
Induction and characterization of a cytochrome P-450-dependent camphor hydroxylase in tissue cultures of common sage (Salvia officinalis)
Plant Physiol.
101
1231-1237
1993
Salvia officinalis
brenda
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1.14.13.161 (+)-camphor 6-exo-hydroxylase
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