ExplorEnz: Search Results

1.14.11.50

Transferred entry:

(–)-deoxypodophyllotoxin synthase. Now EC 1.14.20.8, (–)-deoxypodophyllotoxin synthase

[EC 1.14.11.50 created 2016, deleted 2018]

1.14.13.214

Transferred entry:

(–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase. Now EC 1.14.14.132, (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase

[EC 1.14.13.214 created 2016, deleted 2018]

1.14.20.8

Relevance: 99.4%

Accepted name:

(–)-deoxypodophyllotoxin synthase

Reaction:

(–)-yatein + 2-oxoglutarate + O₂ = (–)-deoxypodophyllotoxin + succinate + CO₂ + H₂O

Glossary:

(–)-yatein = (3R,4R)-4-(1,3-benzodioxol-5-ylmethyl)-3-(3,4,5-trimethoxybenzyl)dihydrofuran-2(3H)-one
(–)-deoxypodophyllotoxin = (5R,5aR,8aR)-5-(3,4,5-trimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3′,4′:6,7]naphtho[2,3-d][1,3]dioxol-6(5a)-one

Other name(s):

2-ODD (gene name)

Systematic name:

(–)-yatein,2-oxoglutarate:oxygen oxidoreductase (ring-forming)

Comments:

The enzyme, characterized from the plant Sinopodophyllum hexandrum (mayapple), is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs. It catalyses the closure of the central six-membered ring in the aryltetralin scaffold.

References:

1.	Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224–1228. [PMID: 26359402]

[EC 1.14.20.8 created 2016 as EC 1.14.11.50, transferred 2018 to EC 1.14.20.8]

1.14.14.132

Relevance: 91.5%

Accepted name:

(–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase

Reaction:

(–)-4′-demethyldeoxypodophyllotoxin + [reduced NADPH—hemoprotein reductase] + O₂ = (–)-4′-demethylepipodophyllotoxin + [oxidized NADPH—hemoprotein reductase] + H₂O

Glossary:

(–)-4′-demethyldeoxypodophyllotoxin = (5R,5aR,8aR)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3′,4′:6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
(–)-4′-demethylepipodophyllotoxin = (5R,5aR,8aR,9S)-9-hydroxy-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3′,4′:6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one

Other name(s):

CYP82D61 (gene name)

Systematic name:

(–)-deoxypodophyllotoxin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)

Comments:

A cytochrome P-450 (heme-thiolate) protein characterized from the plant Sinopodophyllum hexandrum. The enzyme produces the direct precursor to etoposide, a potent anticancer drug. It can also act on (–)-deoxypodophyllotoxin with lower efficiency.

References:

1.	Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224–1228. [PMID: 26359402]

[EC 1.14.14.132 created 2016 as EC 1.14.13.214, transferred 2018 to EC 1.14.14.132]

5.3.3.11

Relevance: 45.4%

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:

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]

1.1.1.243

Relevance: 42.8%

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]

4.2.3.186

Relevance: 40.9%

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]

[EC 4.2.3.186 created 2017]

5.5.1.28

Relevance: 40.8%

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]

[EC 5.5.1.28 created 2017]

4.2.3.95

Relevance: 40.6%

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]

[EC 4.2.3.95 created 2012]

4.2.3.6

Relevance: 39.3%

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]

[EC 4.2.3.6 created 1989 as EC 4.1.99.6, transferred 2000 to EC 4.2.3.6]

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]

1.3.99.25

Relevance: 38.7%

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]

[EC 1.3.99.25 created 2008]

1.1.1.296

Relevance: 38.4%

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]

[EC 1.1.1.296 created 2008]

1.23.1.3

Relevance: 37.1%

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]

[EC 1.23.1.3 created 2013]

1.14.13.47

Transferred entry:

(S)-limonene 3-monooxygenase. Now EC 1.14.14.99, (S)-limonene 3-monooxygenase

[EC 1.14.13.47 created 1992, modified 2003, deleted 2018]

3.1.1.83

Relevance: 36.3%

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]

[EC 3.1.1.83 created 2008]

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]

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]

1.14.13.105

Relevance: 30.8%

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]

[EC 1.14.13.105 created 2008]