EC |
1.3.99.25 | Relevance: 100% |
Accepted name: |
carvone reductase |
Reaction: |
(1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor (2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor |
Glossary: |
(+)-dihydrocarvone = (1S,4R)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
(–)-carvone = (4R)-mentha-1(6),8-dien-6-one = (5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-one |
Systematic name: |
(+)-dihydrocarvone:acceptor 1,6-oxidoreductase |
Comments: |
This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme has not been purified, and requires an unknown cofactor, which is different from NAD+, NADP+ or a flavin. |
References: |
1. |
van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640] |
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[EC 1.3.99.25 created 2008] |
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EC |
1.1.1.243 | Relevance: 82.4% |
Accepted name: |
carveol dehydrogenase |
Reaction: |
(–)-trans-carveol + NADP+ = (–)-carvone + NADPH + H+ |
Other name(s): |
(–)-trans-carveol dehydrogenase |
Systematic name: |
(–)-trans-carveol:NADP+ oxidoreductase |
References: |
1. |
Gershenzon, J., Maffei, M. and Croteau, R. Biochemical and histochemical-localization of monoterpene biosynthesis in the glandular trichomes of spearmint (Mentha spicata). Plant Physiol. 89 (1989) 1351–1357. [PMID: 16666709] |
|
[EC 1.1.1.243 created 1992] |
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EC |
5.3.3.11 | Relevance: 65.6% |
Accepted name: |
isopiperitenone Δ-isomerase |
Reaction: |
isopiperitenone = piperitenone |
Systematic name: |
isopiperitenone Δ8-Δ4-isomerase |
Comments: |
Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves. |
References: |
1. |
Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49–60. [PMID: 3885858] |
|
[EC 5.3.3.11 created 1989] |
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|
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EC |
1.1.1.275 | Relevance: 64.1% |
Accepted name: |
(+)-trans-carveol dehydrogenase |
Reaction: |
(+)-trans-carveol + NAD+ = (+)-(S)-carvone + NADH + H+ |
Other name(s): |
carveol dehydrogenase |
Systematic name: |
(+)-trans-carveol:NAD+ oxidoreductase |
Comments: |
NADP+ cannot replace NAD+. Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds. |
References: |
1. |
Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901–912. [PMID: 9662532] |
|
[EC 1.1.1.275 created 2003] |
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|
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EC
|
1.14.13.80
|
Transferred entry: | (R)-limonene 6-monooxygenase. Now classified as EC 1.14.14.53, (R)-limonene 6-monooxygenase
|
[EC 1.14.13.80 created 2003, deleted 2017] |
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EC
|
1.14.13.104
|
Transferred entry: | (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase
|
[EC 1.14.13.104 created 2008, deleted 2018] |
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|
|
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EC |
1.1.1.296 | Relevance: 55.4% |
Accepted name: |
dihydrocarveol dehydrogenase |
Reaction: |
menth-8-en-2-ol + NAD+ = menth-8-en-2-one + NADH + H+ |
Glossary: |
(+)-dihydrocarveol = (1S,2S,4S)-menth-8-en-2-ol
(+)-isodihydrocarveol = (1S,2S,4R)-menth-8-en-2-ol
(+)-neoisodihydrocarveol = (1S,2R,4R)-menth-8-en-2-ol
(–)-dihydrocarvone = (1S,4S)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one |
Other name(s): |
carveol dehydrogenase (ambiguous) |
Systematic name: |
menth-8-en-2-ol:NAD+ oxidoreductase |
Comments: |
This enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway. The enzyme accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others. The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (–)-isodihydrocarveol. |
References: |
1. |
van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640] |
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[EC 1.1.1.296 created 2008] |
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EC |
1.14.14.53 | Relevance: 53% |
Accepted name: |
(R)-limonene 6-monooxygenase |
Reaction: |
(R)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (+)-trans-carveol + [oxidized NADPH—hemoprotein reductase] + H2O |
Glossary: |
limonene = a monoterpenoid
(R)-limonene = (+)-limonene |
Other name(s): |
(+)-limonene-6-hydroxylase; (+)-limonene 6-monooxygenase |
Systematic name: |
(R)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating) |
Comments: |
The reaction is stereospecific with over 95% yield of (+)-trans-carveol from (R)-limonene. (S)-Limonene, the substrate for EC 1.14.14.51, (S)-limonene 6-monooxygenase, is not a substrate. Forms part of the carvone biosynthesis pathway in Carum carvi (caraway) seeds. |
References: |
1. |
Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901–912. [PMID: 9662532] |
2. |
Bouwmeester, H.J., Konings, M.C.J.M., Gershenzon, J., Karp, F. and Croteau, R. Cytochrome P-450 dependent (+)-limonene-6-hydroxylation in fruits of caraway (Carum carvi). Phytochemistry 50 (1999) 243–248. |
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[EC 1.14.14.53 created 2003 as EC 1.14.13.80, transferred 2017 to EC 1.14.14.53] |
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EC
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1.14.13.47
|
Transferred entry: | (S)-limonene 3-monooxygenase. Now EC 1.14.14.99, (S)-limonene 3-monooxygenase
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[EC 1.14.13.47 created 1992, modified 2003, deleted 2018] |
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EC |
3.1.1.83 | Relevance: 52.5% |
Accepted name: |
monoterpene ε-lactone hydrolase |
Reaction: |
(1) isoprop(en)ylmethyloxepan-2-one + H2O = 6-hydroxyisoprop(en)ylmethylhexanoate (general reaction) (2) 4-isopropenyl-7-methyloxepan-2-one + H2O = 6-hydroxy-3-isopropenylheptanoate (3) 7-isopropyl-4-methyloxepan-2-one + H2O = 6-hydroxy-3,7-dimethyloctanoate |
Other name(s): |
MLH |
Systematic name: |
isoprop(en)ylmethyloxepan-2-one lactonohydrolase |
Comments: |
The enzyme catalyses the ring opening of ε-lactones which are formed during degradation of dihydrocarveol by the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme also acts on ethyl caproate, indicating that it is an esterase with a preference for lactones (internal cyclic esters). The enzyme is not stereoselective. |
References: |
1. |
van der Vlugt-Bergmans , C.J. and van der Werf , M.J. Genetic and biochemical characterization of a novel monoterpene ε-lactone hydrolase from Rhodococcus erythropolis DCL14. Appl. Environ. Microbiol. 67 (2001) 733–741. [PMID: 11157238] |
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[EC 3.1.1.83 created 2008] |
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EC
|
1.14.13.48
|
Transferred entry: | (S)-limonene 6-monooxygenase. Now classified as EC 1.14.14.51, (S)-limonene 6-monooxygenase
|
[EC 1.14.13.48 created 1992, modified 2003, deleted 2017] |
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EC
|
1.14.13.49
|
Transferred entry: | (S)-limonene 7-monooxygenase. Now classified as EC 1.14.14.52, (S)-limonene 7-monooxygenase
|
[EC 1.14.13.49 created 1992, modified 2003, deleted 2017] |
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|
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EC |
4.2.3.20 | Relevance: 50.5% |
Accepted name: |
(R)-limonene synthase |
Reaction: |
geranyl diphosphate = (R)-limonene + diphosphate |
Glossary: |
(R)-limonene = (+)-limonene |
Other name(s): |
(+)-limonene synthase; geranyldiphosphate diphosphate lyase [(+)-(R)-limonene-forming]; geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-(4R)-limonene-forming] |
Systematic name: |
geranyl-diphosphate diphosphate-lyase [cyclizing, (R)-limonene-forming] |
Comments: |
Forms the first step of carvone biosynthesis in caraway. The enzyme from Carum carvi (caraway) seeds requires a divalent metal ion (preferably Mn2+) for catalysis. This enzyme occurs in Citrus, Carum (caraway) and Anethum (dill); (-)-limonene, however, is made in the fir, Abies, and mint, Mentha, by EC 4.2.3.16, (4S)-limonene synthase. |
References: |
1. |
Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901–912. [PMID: 9662532] |
2. |
Lücker, J., El Tamer, M.K., Schwab, W., Verstappen, F.W., van der Plas, L.H., Bouwmeester, H.J. and Verhoeven, H.A. Monoterpene biosynthesis in lemon (Citrus limon). cDNA isolation and functional analysis of four monoterpene synthases. Eur. J. Biochem. 269 (2000) 3160–3171. [PMID: 12084056] |
3. |
Maruyama, T., Ito, M., Kiuchi, F. and Honda, G. Molecular cloning, functional expression and characterization of d-limonene synthase from Schizonepeta tenuifolia. Biol. Pharm. Bull. 24 (2001) 373–377. [PMID: 11305598] |
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[EC 4.2.3.20 created 2003] |
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EC |
1.14.13.105 | Relevance: 44.4% |
Accepted name: |
monocyclic monoterpene ketone monooxygenase |
Reaction: |
(1) (–)-menthone + NADPH + H+ + O2 = (4R,7S)-7-isopropyl-4-methyloxepan-2-one + NADP+ + H2O (2) dihydrocarvone + NADPH + H+ + O2 = 4-isopropenyl-7-methyloxepan-2-one + NADP+ + H2O (3) (iso)-dihydrocarvone + NADPH + H+ + O2 = 6-isopropenyl-3-methyloxepan-2-one + NADP+ + H2O (4a) 1-hydroxymenth-8-en-2-one + NADPH + H+ + O2 = 7-hydroxy-4-isopropenyl-7-methyloxepan-2-one + NADP+ + H2O (4b) 7-hydroxy-4-isopropenyl-7-methyloxepan-2-one = 3-isopropenyl-6-oxoheptanoate (spontaneous) |
Other name(s): |
1-hydroxy-2-oxolimonene 1,2-monooxygenase; dihydrocarvone 1,2-monooxygenase; MMKMO |
Systematic name: |
(–)-menthone,NADPH:oxygen oxidoreductase |
Comments: |
A flavoprotein (FAD). This Baeyer-Villiger monooxygenase enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 has wide substrate specificity, catalysing the lactonization of a large number of monocyclic monoterpene ketones and substituted cyclohexanones [2]. Both (1R,4S)- and (1S,4R)-1-hydroxymenth-8-en-2-one are metabolized, with the lactone product spontaneously rearranging to form 3-isopropenyl-6-oxoheptanoate [1]. |
References: |
1. |
van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092–2102. [PMID: 10224006] |
2. |
Van Der Werf, M.J. Purification and characterization of a Baeyer-Villiger mono-oxygenase from Rhodococcus erythropolis DCL14 involved in three different monocyclic monoterpene degradation pathways. Biochem. J. 347 (2000) 693–701. [PMID: 10769172] |
3. |
van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640] |
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[EC 1.14.13.105 created 2008] |
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|
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EC |
1.1.1.223 | Relevance: 30.6% |
Accepted name: |
isopiperitenol dehydrogenase |
Reaction: |
(-)-trans-isopiperitenol + NAD+ = (-)-isopiperitenone + NADH + H+ |
Systematic name: |
(-)-trans-isopiperitenol:NAD+ oxidoreductase |
Comments: |
Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol. Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves. |
References: |
1. |
Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49–60. [PMID: 3885858] |
|
[EC 1.1.1.223 created 1989] |
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|
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EC |
5.5.1.28 | Relevance: 30% |
Accepted name: |
(–)-kolavenyl diphosphate synthase |
Reaction: |
geranylgeranyl diphosphate = (–)-kolavenyl diphosphate |
Glossary: |
(–)-kolavenyl diphosphate = (2E)-5-[(1R,2S,4aS,8aS)-1,2,4a,5-tetramethyl-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-yl]-3-methylpent-2-en-1-yl diposphate |
Other name(s): |
SdKPS; TwTPS14; TwTPS10/KPS; SdCPS2; clerodienyl diphosphate synthase; CLPP |
Systematic name: |
(–)-kolavenyl diphosphate lyase (ring-opening) |
Comments: |
Isolated from the hallucinogenic plant Salvia divinorum (seer’s sage) and the medicinal plant Tripterygium wilfordii (thunder god vine). |
References: |
1. |
Hansen, N.L., Heskes, A.M., Hamberger, B., Olsen, C.E., Hallstrom, B.M., Andersen-Ranberg, J. and Hamberger, B. The terpene synthase gene family in Tripterygium wilfordii harbors a labdane-type diterpene synthase among the monoterpene synthase TPS-b subfamily. Plant J. 89 (2017) 429–441. [PMID: 27801964] |
2. |
Chen, X., Berim, A., Dayan, F.E. and Gang, D.R. A (–)-kolavenyl diphosphate synthase catalyzes the first step of salvinorin A biosynthesis in Salvia divinorum. J. Exp. Bot. 68 (2017) 1109–1122. [PMID: 28204567] |
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[EC 5.5.1.28 created 2017] |
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|
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EC |
4.2.3.186 | Relevance: 30% |
Accepted name: |
ent-13-epi-manoyl oxide synthase |
Reaction: |
ent-8α-hydroxylabd-13-en-15-yl diphosphate = ent-13-epi-manoyl oxide + diphosphate |
Glossary: |
Ent-13-epi-manoyl oxide = (13R)-ent-8,13-epoxylabd-14-ene |
Other name(s): |
SmKSL2; ent-LDPP synthase |
Systematic name: |
ent-8α-hydroxylabd-13-en-15-yl-diphosphate diphosphate-lyase (cyclizing, ent-13-epi-manoyl-oxide-forming) |
Comments: |
Isolated from the plant Salvia miltiorrhiza (red sage). |
References: |
1. |
Cui, G., Duan, L., Jin, B., Qian, J., Xue, Z., Shen, G., Snyder, J.H., Song, J., Chen, S., Huang, L., Peters, R.J. and Qi, X. Functional divergence of diterpene syntheses in the medicinal plant Salvia miltiorrhiza. Plant Physiol. 169 (2015) 1607–1618. [PMID: 26077765] |
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[EC 4.2.3.186 created 2017] |
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|
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EC |
4.2.3.95 | Relevance: 29.8% |
Accepted name: |
(-)-α-cuprenene synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = (-)-α-cuprenene + diphosphate |
Other name(s): |
Cop6 |
Systematic name: |
(-)-α-cuprenene hydrolase [cyclizing, (-)-α-cuprenene-forming] |
Comments: |
The enzyme from the fungus Coprinopsis cinerea produces (-)-α-cuprenene with high selectivity. |
References: |
1. |
Lopez-Gallego, F., Agger, S.A., Abate-Pella, D., Distefano, M.D. and Schmidt-Dannert, C. Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers. ChemBioChem 11 (2010) 1093–1106. [PMID: 20419721] |
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[EC 4.2.3.95 created 2012] |
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|
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EC |
1.1.1.144 | Relevance: 29.6% |
Accepted name: |
perillyl-alcohol dehydrogenase |
Reaction: |
perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+ |
Other name(s): |
perillyl alcohol dehydrogenase |
Systematic name: |
perillyl-alcohol:NAD+ oxidoreductase |
Comments: |
Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic. |
References: |
1. |
Ballal, N.R., Bhattacharyya, P.K. and Rangachari, P.N. Perillyl alcohol dehydrogenase from a soil pseudomonad. Biochem. Biophys. Res. Commun. 23 (1966) 473–478. [PMID: 4289759] |
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[EC 1.1.1.144 created 1972] |
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|
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EC |
4.2.3.6 | Relevance: 28.8% |
Accepted name: |
trichodiene synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate |
Other name(s): |
trichodiene synthetase; sesquiterpene cyclase; trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming) |
References: |
1. |
Hohn, T.M. and Vanmiddlesworth, F. Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides. Arch. Biochem. Biophys. 251 (1986) 756–761. [PMID: 3800398] |
2. |
Hohn, T.M. and Beremand, P.D. Isolation and nucleotide sequence of a sesquiterpene cyclase gene from the trichothecene-producing fungus Fusarium sporotrichioides. Gene 79 (1989) 131–138. [PMID: 2777086] |
3. |
Rynkiewicz, M.J., Cane, D.E. and Christianson, D.W. Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade. Proc. Natl. Acad. Sci. USA 98 (2001) 13543–13548. [PMID: 11698643] |
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[EC 4.2.3.6 created 1989 as EC 4.1.99.6, transferred 2000 to EC 4.2.3.6] |
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EC |
1.23.1.3 | Relevance: 27.3% |
Accepted name: |
(–)-pinoresinol reductase |
Reaction: |
(–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+ |
Glossary: |
(–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol) |
Other name(s): |
pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR |
Systematic name: |
(–)-lariciresinol:NADP+ oxidoreductase |
Comments: |
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3]. |
References: |
1. |
Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [PMID: 9872995] |
2. |
Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [PMID: 17257599] |
3. |
Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [PMID: 18347017] |
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[EC 1.23.1.3 created 2013] |
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|
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EC |
1.3.1.82 | Relevance: 26.4% |
Accepted name: |
(-)-isopiperitenone reductase |
Reaction: |
(+)-cis-isopulegone + NADP+ = (-)-isopiperitenone + NADPH + H+ |
Systematic name: |
(+)-cis-isopulegone:NADP+ oxidoreductase |
Comments: |
The reaction occurs in the opposite direction to that shown above. The enzyme participates in the menthol-biosynthesis pathway of Mentha plants. (+)-Pulegone, (+)-cis-isopulegone and (-)-menthone are not substrates. The enzyme has a preference for NADPH as the reductant, with NADH being a poor substitute [2]. The enzyme is highly regioselective for the reduction of the endocyclic 1,2-double bond, and is stereoselective, producing only the 1R-configured product. It is a member of the short-chain dehydrogenase/reductase superfamily. |
References: |
1. |
Croteau, R. and Venkatachalam, K.V. Metabolism of monoterpenes: demonstration that (+)-cis-isopulegone, not piperitenone, is the key intermediate in the conversion of (-)-isopiperitenone to (+)-pulegone in peppermint (Mentha piperita). Arch. Biochem. Biophys. 249 (1986) 306–315. [PMID: 3755881] |
2. |
Ringer, K.L., McConkey, M.E., Davis, E.M., Rushing, G.W. and Croteau, R. Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint. Arch. Biochem. Biophys. 418 (2003) 80–92. [PMID: 13679086] |
|
[EC 1.3.1.82 created 2008] |
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|
|
|
EC |
1.14.14.51 | Relevance: 24.8% |
Accepted name: |
(S)-limonene 6-monooxygenase |
Reaction: |
(S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-trans-carveol + [oxidized NADPH—hemoprotein reductase] + H2O |
Glossary: |
limonene = a monoterpenoid
(S)-limonene = (–)-limonene |
Other name(s): |
(–)-limonene 6-hydroxylase; (–)-limonene 6-monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating) |
Systematic name: |
(S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating) |
Comments: |
A cytochrome P-450 (heme thiolate) enzyme. The enzyme participates in the biosynthesis of (–)-carvone, which is responsible for the aroma of spearmint. |
References: |
1. |
Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219–226. [PMID: 2297225] |
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[EC 1.14.14.51 created 1992 as EC 1.14.13.48, modified 2003, transferred 2017 to EC 1.14.14.51] |
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EC |
1.14.14.143 | Relevance: 24.8% |
Accepted name: |
(+)-menthofuran synthase |
Reaction: |
(+)-pulegone + [reduced NADPH—hemoprotein reductase] + O2 = (+)-menthofuran + [oxidized NADPH—hemoprotein reductase] + H2O |
Other name(s): |
menthofuran synthase; (+)-pulegone 9-hydroxylase; (+)-MFS; cytochrome P450 menthofuran synthase |
Systematic name: |
(+)-pulegone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. The conversion of substrate into product involves the hydroxylation of the syn-methyl (C9), intramolecular cyclization to the hemiketal and dehydration to the furan [1]. This is the second cytochrome P-450-mediated step of monoterpene metabolism in peppermint, with the other step being catalysed by EC 1.14.14.99, (S)-limonene 3-monooxygenase [1]. |
References: |
1. |
Bertea, C.M., Schalk, M., Karp, F., Maffei, M. and Croteau, R. Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene. Arch. Biochem. Biophys. 390 (2001) 279–286. [PMID: 11396930] |
2. |
Mahmoud, S.S. and Croteau, R.B. Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 14481–14486. [PMID: 14623962] |
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[EC 1.14.14.143 created 2008 as EC 1.14.13.104, transferred 2018 to EC 1.14.14.143] |
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