Information on EC 1.14.14.52 - (S)-limonene 7-monooxygenase

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oxygenase, (-)-limonene mono-

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additional information

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the enzyme is a cytochrome P450 limonene hydroxylase

(S)-limonene + [reduced NADPH-hemoprotein reductase] + O2 = (-)-perillyl alcohol + [oxidized NADPH-hemoprotein reductase] + H2O

Biosynthesis of secondary metabolites, Limonene and pinene degradation, Monoterpenoid biosynthesis

oxidation

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redox reaction

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reduction

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KEGG

MetaCyc

perillyl aldehyde biosynthesis

(S)-limonene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (7-hydroxylating)

A cytochrome P-450 (heme thiolate) enzyme. The enzyme, characterized from the plant Perilla frutescens, participates in the biosynthesis of perillyl aldehyde, the major constituent of the essential oil that accumulates in the glandular trichomes of this plant. Some forms of the enzyme also catalyse the oxidation of (-)-perillyl alcohol to (-)-perillyl aldehyde.

122653-75-2

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(+)-limonene + NADPH + O2

perillyl alcohol + NADP+ + H2O

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hydroxylation at the same rate as (-)-limonene

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?

(-)-(S)-limonene + NADPH + O2

(-)-perillyl alcohol + NADP+ + H2O

(-)-limonene + NADPH + O2

perillyl alcohol + NADP+ + H2O

(S)-limonene + NADPH + H+ + O2

(-)-perillyl alcohol + NADP+ + H2O

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additional information

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(-)-(S)-limonene + NADPH + O2

(-)-perillyl alcohol + NADP+ + H2O

(-)-limonene + NADPH + O2

perillyl alcohol + NADP+ + H2O

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one of the key reactions of oxygenated monoterpenes, perillyl aldehyde biosynthesis

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(S)-limonene + NADPH + H+ + O2

(-)-perillyl alcohol + NADP+ + H2O

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cytochrome P450

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heme-thiolate protein, 0.2-0.9 nmol per mg protein

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NADH

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5.3% as effective as NADPH

NADPH

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390083, 713236

5,11-Dimethyl-6H-pyrido[4,3-b]carbazole

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clotrimazole

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i.e. 1-[chloro-alpha,alpha-diphenyl]imidazole, mixed-type, weak

CO

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CO:O2 ratio of 9:1, photoreversible

cytochrome c

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strong

Metyrapone

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i.e. 2-methyl-1,2-di-3-pyridyl-1-propanone, moderate

miconazole

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i.e. 1-[2,4-dichloro-beta-([2,4-di-chlorobenzyl]oxy)phenethyl]-imidazole, mixed-type, weak

NADP+

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2 mM

SKF 525A

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i.e. 2-diethyl-aminoethyl-2,2-diphenylvalerate, moderate

additional information

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no inhibition: ancymidol, imidazole, up to 5 mM

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FAD

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plus FMN, 0.005 mM each, activation

FMN

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plus FAD, 0.005 mM each, activation

0.021

(-)-limonene

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0.0001567

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7

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7.6

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recombinant chimeric mutant enzyme

7.8

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5.5 - 8

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almost no activity at pH 5.5 and pH 8.0, respectively

6.75 - 8.5

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half-maximal activity at pH 6.75 and 8.5, recombinant chimeric mutant enzyme

7.3 - 8.3

Mycobacterium sp. HXN-1500

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about half-maximal activity at pH 7.3 and 8.3

32

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HXN-1500

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HXN-1500

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oil glands on abaxial surface

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Homo sapiens

48000

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x * 48000, SDS-PAGE

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additional information

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construction of a chimeric mutant enzyme by fusion of the N-terminal membrane insertion domain of the limonene-3-hydroxylase into limonene 7-hydroxylase. The kinetically competent recombinant protein produces a mixture of C3-, C6- and C7-hydroxylated limonene derivatives with a distribution of 33%, 14% and 53%, respectively

0

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50% loss of activity after 6 h

ammonium sulfate, phenyl Sepharose, Source Q15

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DNA and amino acid sequence determination and analysis, expression in Escherichia coli as a chimeric protein fused with the N-terminal membrane insertion domain of the limonene-3-hydroxylase

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expression in n-octane grown Pseudomonas putida

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