EC |
2.5.1.67 | Relevance: 100% |
Accepted name: |
chrysanthemyl diphosphate synthase |
Reaction: |
2 prenyl diphosphate = diphosphate + chrysanthemyl diphosphate |
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For diagram of reaction, click here |
Glossary: |
chrysanthemyl = [2,2-dimethyl-3-(2-methylprop-1-en-1-yl)cyclopropyl]methyl
chrysanthemic acid = 2,2-dimethyl-3-(2-methylprop-1-en-1-yl)cyclopropane-1-carboxylic acid |
Other name(s): |
CPPase; dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl-diphosphate-forming) |
Systematic name: |
prenyl-diphosphate:prenyl-diphosphate prenyltransferase (chrysanthemyl-diphosphate-forming) |
Comments: |
Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+ [1]. Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Rivera, S.B., Swedlund, B.D., King, G.J., Bell, R.N., Hussey, C.E., Jr., Shattuck-Eidens, D.M., Wrobel, W.M., Peiser, G.D. and Poulter, C.D. Chrysanthemyl diphosphate synthase: isolation of the gene and characterization of the recombinant non-head-to-tail monoterpene synthase from Chrysanthemum cinerariaefolium. Proc. Natl. Acad. Sci. USA 98 (2001) 4373–4378. [DOI] [PMID: 11287653] |
2. |
Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886–6888. [DOI] [PMID: 12783539] |
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[EC 2.5.1.67 created 2007] |
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EC
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2.5.1.99
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Deleted entry: | all-trans-phytoene synthase. The activity was an artifact caused by photoisomerization of the product of EC 2.5.1.32, 15-cis-phytoene synthase. |
[EC 2.5.1.99 created 2012, deleted 2018] |
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EC |
4.2.3.187 | Relevance: 99.5% |
Accepted name: |
(2Z,6E)-hedycaryol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = (2Z,6E)-hedycaryol + diphosphate |
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For diagram of biosynthesis of ent-germacrene sesquiterpenoids, click here |
Glossary: |
(2Z,6E)-hedycaryol = (1E,4Z,7S)-germacra-1(10),4-dien-11-ol |
Other name(s): |
HcS |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [cyclizing, (2Z,6E)-hedycaryol-forming] |
Comments: |
Isolated from the bacterium Kitasatospora setae. The stereochemistry suggests the farnesyl diphosphate rearranges to nerolidyl diphosphate or an equivalent intermediate before cyclization. See also EC 4.2.3.174 (2E,6E)-hedycaryol synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Baer, P., Rabe, P., Citron, C.A., de Oliveira Mann, C.C., Kaufmann, N., Groll, M. and Dickschat, J.S. Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism. ChemBioChem 15 (2014) 213–216. [DOI] [PMID: 24399794] |
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[EC 4.2.3.187 created 2017] |
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EC |
2.7.4.6 | Relevance: 99.3% |
Accepted name: |
nucleoside-diphosphate kinase |
Reaction: |
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate |
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For diagram of GTP biosynthesis, click here |
Other name(s): |
nucleoside 5′-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase |
Systematic name: |
ATP:nucleoside-diphosphate phosphotransferase |
Comments: |
Many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-51-1 |
References: |
1. |
Berg, P. and Joklik, W.K. Enzymatic phosphorylation of nucleoside diphosphates. J. Biol. Chem. 210 (1954) 657–672. [PMID: 13211603] |
2. |
Gibson, D.M., Ayengar, P. and Sanadi, D.R. Transphosphorylations between nucleoside phosphates. Biochim. Biophys. Acta 21 (1956) 86–91. [DOI] [PMID: 13363863] |
3. |
Kirkland, R.J.A. and Turner, J.F. Nucleoside diphosphokinase of pea seeds. Biochem. J. 72 (1959) 716–720. [PMID: 14409347] |
4. |
Krebs, H.A. and Hems, R. Some reactions of adenosine and inosine phosphates in animal tissues. Biochim. Biophys. Acta 12 (1953) 172–180. [DOI] [PMID: 13115426] |
5. |
Nakamura, H. and Sugino, Y. Metabolism of deoxyribonucleotides. 3. Purification and some properties of nucleoside diphosphokinase of calf thymus. J. Biol. Chem. 241 (1966) 4917–4922. [PMID: 5925862] |
6. |
Ratliff, R.L., Weaver, R.H., Lardy, H.A. and Kuby, S.A. Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). I. Isolation of the crystalline enzyme from brewers' yeast. J. Biol. Chem. 239 (1964) 301–309. [PMID: 14114857] |
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[EC 2.7.4.6 created 1961] |
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EC |
2.5.1.81 | Relevance: 98.5% |
Accepted name: |
geranylfarnesyl diphosphate synthase |
Reaction: |
geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate |
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For diagram of terpenoid biosynthesis, click here |
Other name(s): |
FGPP synthase; (all-E) geranylfarnesyl diphosphate synthase; GFPS; Fgs |
Systematic name: |
geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit) |
Comments: |
The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate [1]. The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ogawa, T., Yoshimura, T. and Hemmi, H. Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution. Biochem. Biophys. Res. Commun. 393 (2010) 16–20. [DOI] [PMID: 20097171] |
2. |
Tachibana, A., Yano, Y., Otani, S., Nomura, N., Sako, Y. and Taniguchi, M. Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur. J. Biochem. 267 (2000) 321–328. [DOI] [PMID: 10632701] |
3. |
Tachibana, A. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett. 341 (1994) 291–294. [DOI] [PMID: 8137956] |
4. |
Lee, P.C., Mijts, B.N., Petri, R., Watts, K.T. and Schmidt-Dannert, C. Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. Protein Eng. Des. Sel. 17 (2004) 771–777. [DOI] [PMID: 15548566] |
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[EC 2.5.1.81 created 2010] |
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EC |
4.2.3.98 | Relevance: 98% |
Accepted name: |
(+)-T-muurolol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = (+)-T-muurolol + diphosphate |
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For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here |
Glossary: |
(+)-T-muurolol = (1R,4R,4aS,8aR)-1,6-dimethyl-4-(propan-2-yl)-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-ol |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-T-muurolol-forming) |
Comments: |
The cyclization mechanism involves an intermediate nerolidyl diphosphate leading to a helminthogermacradienyl cation. After a 1,3-hydride shift of the original 1-pro-S hydrogen of farnesyl diphosphate, cyclization and deprotonation result in (+)-T-muurolol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hu, Y., Chou, W.K., Hopson, R. and Cane, D.E. Genome mining in Streptomyces clavuligerus: expression and biochemical characterization of two new cryptic sesquiterpene synthases. Chem. Biol. 18 (2011) 32–37. [DOI] [PMID: 21276937] |
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[EC 4.2.3.98 created 2012] |
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EC |
4.2.3.19 | Relevance: 97.9% |
Accepted name: |
ent-kaurene synthase |
Reaction: |
ent-copalyl diphosphate = ent-kaurene + diphosphate |
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For diagram of the biosynthesis of copalyl diphosphate, abietadiene and ent-kaurene, click here |
Other name(s): |
ent-kaurene synthase B; ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase (cyclizing) |
Systematic name: |
ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-kaurene-forming) |
Comments: |
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-64-5 |
References: |
1. |
Fall, R.R., West, C.A. Purification and properties of kaurene synthetase from Fusarium moniliforme. J. Biol. Chem. 246 (1971) 6913–6928. [PMID: 4331199] |
2. |
Yamaguchi, S., Saito, T., Abe, H., Yamane, H., Murofushi, N. and Kamiya, Y. Molecular cloning and characterization of a cDNA encoding the gibberellin biosynthetic enzyme ent-kaurene synthase B from pumpkin (Cucurbita maxima L.). Plant J. 10 (1996) 203–213. [DOI] [PMID: 8771778] |
3. |
Kawaide, H., Imai, R., Sassa, T. and Kamiya, Y. Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis. J. Biol. Chem. 272 (1997) 21706–21712. [DOI] [PMID: 9268298] |
4. |
Toyomasu, T., Kawaide, H., Ishizaki, A., Shinoda, S., Otsuka, M., Mitsuhashi, W. and Sassa, T. Cloning of a full-length cDNA encoding ent-kaurene synthase from Gibberella fujikuroi: functional analysis of a bifunctional diterpene cyclase. Biosci. Biotechnol. Biochem. 64 (2000) 660–664. [DOI] [PMID: 10803977] |
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[EC 4.2.3.19 created 2002] |
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EC |
4.2.3.99 | Relevance: 97.2% |
Accepted name: |
labdatriene synthase |
Reaction: |
9α-copalyl diphosphate = (12E)-9α-labda-8(17),12,14-triene + diphosphate |
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For diagram of diterpenoids from 9α-copalyl diphosphate, click here |
Glossary: |
9α-copalyl diphosphate = syn-copalyl diphosphate = (2E)-3-methyl-5-[(1R,4aS,8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]pent-2-en-1-yl trihydrogen diphosphate
(12E)-9α-labda-8(17),12,14-triene = (4aS,5R,8aS)-1,1,4a-trimethyl-6-methylidene-5-[(2E)-3-methylpenta-2,4-dien-1-yl]decahydronaphthalene
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Other name(s): |
OsKSL10 (gene name) |
Systematic name: |
9α-copalyl-diphosphate diphosphate-lyase [(12E)-9α-labda-8(17),12,14-triene-forming] |
Comments: |
The enzyme from rice (Oryza sativa), expressed in Escherichia coli, also produces ent-sandaracopimara-8(14),15-diene from ent-copalyl diphosphate, another naturally occuring copalyl isomer in rice (cf. ent-sandaracopimaradiene synthase, EC 4.2.3.29). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Morrone, D., Hillwig, M.L., Mead, M.E., Lowry, L., Fulton, D.B. and Peters, R.J. Evident and latent plasticity across the rice diterpene synthase family with potential implications for the evolution of diterpenoid metabolism in the cereals. Biochem. J. 435 (2011) 589–595. [DOI] [PMID: 21323642] |
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[EC 4.2.3.99 created 2012] |
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EC |
4.2.3.188 | Relevance: 97.1% |
Accepted name: |
β-geranylfarnesene synthase |
Reaction: |
(1) all-trans-geranylfarnesyl diphosphate = β-geranylfarnesene + diphosphate (2) all-trans-hexaprenyl diphosphate = β-hexaprene + diphosphate (3) all-trans-heptaprenyl diphosphate = β-heptaprene + diphosphate
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|
For diagram of sesquarterpenoid biosynthesis, click here and for diagram of sesterterpenoids biosynthesis, click here |
Glossary: |
β-geranylfarnesene = (6E,10E,14E)-7,11,15,19-tetramethyl-3-methyleneicosa-1,6,10,14,18-pentaene
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Other name(s): |
Bcl-TS |
Systematic name: |
all-trans-geranylfarnesyl-diphosphate diphosphate-lyase (β-geranylfarnesene-forming) |
Comments: |
Isolated from the bacterium Bacillus clausii. The enzyme acts on a range of polyprenyl diphosphates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sato, T., Yamaga, H., Kashima, S., Murata, Y., Shinada, T., Nakano, C. and Hoshino, T. Identification of novel sesterterpene/triterpene synthase from Bacillus clausii. ChemBioChem 14 (2013) 822–825. [DOI] [PMID: 23554321] |
2. |
Ueda, D., Yamaga, H., Murakami, M., Totsuka, Y., Shinada, T. and Sato, T. Biosynthesis of sesterterpenes, head-to-tail triterpenes, and sesquarterpenes in Bacillus clausii: identification of multifunctional enzymes and analysis of isoprenoid metabolites. ChemBioChem 16 (2015) 1371–1377. [DOI] [PMID: 25882275] |
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[EC 4.2.3.188 created 2017] |
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EC |
4.2.3.170 | Relevance: 96.9% |
Accepted name: |
4-epi-cubebol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = 4-epi-cubebol + diphosphate |
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For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here |
Glossary: |
4-epi-cubebol = (3S,3aS,3bR,4S,7S,7aS)-4-(2-hydroxypropan-2-yl)-7-methyloctahydro-1H-cyclopenta[1,3]cyclopropa[1,2]benzen-3-ol |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, 4-epi-cubebol-forming) |
Comments: |
The enzyme, found in the bacterium Streptosporangium roseum, is specific for (2E,6E)-farnesyl diphosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rabe, P., Schmitz, T. and Dickschat, J.S. Mechanistic investigations on six bacterial terpene cyclases. Beilstein J. Org. Chem. 12 (2016) 1839–1850. [DOI] [PMID: 27829890] |
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[EC 4.2.3.170 created 2017] |
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EC
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2.5.1.11
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Transferred entry: | trans-octaprenyltranstransferase. Now covered by EC 2.5.1.84 (all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]) and EC 2.5.1.85 (all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific])
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[EC 2.5.1.11 created 1972, deleted 2010] |
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EC
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1.14.13.104
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Transferred entry: | (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase
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[EC 1.14.13.104 created 2008, deleted 2018] |
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EC |
4.2.3.8 | Relevance: 96.2% |
Accepted name: |
casbene synthase |
Reaction: |
geranylgeranyl diphosphate = casbene + diphosphate |
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For diagram of cembrene and related diterpenoids, click here |
Other name(s): |
casbene synthetase; geranylgeranyl-diphosphate diphosphate-lyase (cyclizing) |
Systematic name: |
geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, casbene-forming) |
Comments: |
The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69106-45-2 |
References: |
1. |
Moesta, P. and West, C.A. Casbene synthetase: regulation of phytoalexin biosynthesis in Ricinus communis L. seedlings. Purification of casbene synthetase and regulation of its biosynthesis during elicitation. Arch. Biochem. Biophys. 238 (1985) 325–333. [DOI] [PMID: 3985625] |
2. |
Mau, C.J. and West, C.A. Cloning of casbene synthase cDNA: evidence for conserved structural features among terpenoid cyclases in plants. Proc. Natl. Acad. Sci. USA 91 (1994) 8497–8501. [DOI] [PMID: 8078910] |
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[EC 4.2.3.8 created 1989 as EC 4.6.1.7, transferred 2000 to EC 4.2.3.8, modified 2024] |
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EC |
1.3.99.25 | Relevance: 96% |
Accepted name: |
carvone reductase |
Reaction: |
(1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor (2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor |
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For diagram of (–)-carvone catabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 10832640] |
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[EC 1.3.99.25 created 2008] |
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EC |
4.2.3.140 | Relevance: 96% |
Accepted name: |
cis-abienol synthase |
Reaction: |
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = cis-abienol + diphosphate |
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For diagram of hydroxylabdenyl diphosphate derived diterpenoids, click here |
Glossary: |
cis-abienol = (12Z)-labda-12,14-dien-8α-ol
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = 8-hydroxycopalyl diphosphate |
Other name(s): |
Z-abienol synthase; CAS; ABS |
Systematic name: |
(13E)-8α-hydroxylabd-13-en-15-yl-diphosphate-lyase (cis-abienol-forming) |
Comments: |
Isolated from the plants Abies balsamea (balsam fir) [1] and Nicotiana tabacum (tobacco) [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Zerbe, P., Chiang, A., Yuen, M., Hamberger, B., Hamberger, B., Draper, J.A., Britton, R. and Bohlmann, J. Bifunctional cis-abienol synthase from Abies balsamea discovered by transcriptome sequencing and its implications for diterpenoid fragrance production. J. Biol. Chem. 287 (2012) 12121–12131. [DOI] [PMID: 22337889] |
2. |
Sallaud, C., Giacalone, C., Topfer, R., Goepfert, S., Bakaher, N., Rosti, S. and Tissier, A. Characterization of two genes for the biosynthesis of the labdane diterpene Z-abienol in tobacco (Nicotiana tabacum) glandular trichomes. Plant J. 72 (2012) 1–17. [DOI] [PMID: 22672125] |
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[EC 4.2.3.140 created 2012] |
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EC |
3.6.1.76 | Relevance: 95.3% |
Accepted name: |
prenyl-diphosphate phosphatase |
Reaction: |
(1) prenyl diphosphate + H2O = prenyl phosphate + phosphate (2) 3-methylbut-3-en-1-yl diphosphate + H2O = 3-methylbut-3-en-1-yl phosphate + phosphate |
Glossary: |
isopentenyl = 3-methylbut-3-en-1-yl
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl
dimethylallyl diphosphate = DMAPP
isopentenyl diphosphate = IPP |
Systematic name: |
prenyl diphosphate/3-methylbut-3-en-1-yl diphosphate phosphohydrolase |
Comments: |
The enzyme, characterized from the methanogenic archaeon Methanosarcina mazei, belongs to the Nudix hydrolase family (a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to a moiety). Its main purpose is to provide the substrate for EC 2.5.1.129, flavin prenyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ishibashi, Y., Matsushima, N., Ito, T. and Hemmi, H. Isopentenyl diphosphate/dimethylallyl diphosphate-specific Nudix hydrolase from the methanogenic archaeon Methanosarcina mazei. Biosci. Biotechnol. Biochem. 86 (2022) 246–253. [DOI] [PMID: 34864834] |
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[EC 3.6.1.76 created 2022] |
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EC |
1.1.1.296 | Relevance: 95.3% |
Accepted name: |
dihydrocarveol dehydrogenase |
Reaction: |
menth-8-en-2-ol + NAD+ = menth-8-en-2-one + NADH + H+ |
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For diagram of (–)-carvone catabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 10832640] |
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[EC 1.1.1.296 created 2008] |
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|
EC |
4.2.3.116 | Relevance: 95.3% |
Accepted name: |
(+)-camphene synthase |
Reaction: |
geranyl diphosphate = (+)-camphene + diphosphate |
Glossary: |
(+)-camphene = (1R,4S)-2,2-dimethyl-3-methylenebicyclo[2.2.1]heptane |
Systematic name: |
geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-camphene-forming] |
Comments: |
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-camphene and (+)-α-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. Requires Mg2+ (preferred to Mn2+). See also EC 4.2.3.121 (+)-α-pinene synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gambliel, H. and Croteau, R. Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration. J. Biol. Chem. 259 (1984) 740–748. [PMID: 6693393] |
2. |
Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene. J. Biol. Chem. 263 (1988) 10063–10071. [PMID: 3392006] |
3. |
Wagschal, K.C., Pyun, H.J., Coates, R.M. and Croteau, R. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 477–487. [DOI] [PMID: 8109978] |
4. |
Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [DOI] [PMID: 8109979] |
|
[EC 4.2.3.116 created 2012] |
|
|
|
|
EC |
4.2.3.144 | Relevance: 95.1% |
Accepted name: |
geranyllinalool synthase |
Reaction: |
geranylgeranyl diphosphate + H2O = (6E,10E)-geranyllinalool + diphosphate |
|
For diagram of acyclic diterpenoid biosynthesis, click here |
Glossary: |
geranylgeranyl diphosphate = (2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraen-1-yl diphosphate
(6E,10E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol |
Other name(s): |
TPS04/GES; GES |
Systematic name: |
geranylgeranyl-diphosphate diphosphate-lyase [(E,E)-geranyllinalool-forming] |
Comments: |
The enzyme is a component of the herbivore-induced indirect defense system. The product, (E,E)-geranyllinalool, is a precursor to the volatile compound 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT), which is released by many plants in response to damage. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Herde, M., Gartner, K., Kollner, T.G., Fode, B., Boland, W., Gershenzon, J., Gatz, C. and Tholl, D. Identification and regulation of TPS04/GES, an Arabidopsis geranyllinalool synthase catalyzing the first step in the formation of the insect-induced volatile C16-homoterpene TMTT. Plant Cell 20 (2008) 1152–1168. [DOI] [PMID: 18398052] |
2. |
Attaran, E., Rostas, M. and Zeier, J. Pseudomonas syringae elicits emission of the terpenoid (E,E)-4,8,12-trimethyl-1,3,7,11-tridecatetraene in Arabidopsis leaves via jasmonate signaling and expression of the terpene synthase TPS4. Mol. Plant Microbe Interact. 21 (2008) 1482–1497. [DOI] [PMID: 18842097] |
|
[EC 4.2.3.144 created 2013] |
|
|
|
|
EC |
4.2.3.190 | Relevance: 95% |
Accepted name: |
manoyl oxide synthase |
Reaction: |
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = manoyl oxide + diphosphate |
|
For diagram of hydroxylabdenyl diphosphate derived diterpenoids, click here |
Glossary: |
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = 8-hydroxycopalyl diphosphate
manoyl oxide = (13R)-8,13-epoxylabd-14-ene |
Other name(s): |
GrTPS6; CfTPS3; CfTPS4; MvELS |
Systematic name: |
(13E)-8α-hydroxylabd-13-en-15-yl-diphosphate diphosphate-lyase (manoyl-oxide-forming) |
Comments: |
Manoyl oxide is found in many plants. This enzyme has been isolated from the plants, Grindelia hirsutula (gum weed), Plectranthus barbatus (forskohlii) and Marrubium vulgare (white horehound). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Zerbe, P., Hamberger, B., Yuen, M.M., Chiang, A., Sandhu, H.K., Madilao, L.L., Nguyen, A., Hamberger, B., Bach, S.S. and Bohlmann, J. Gene discovery of modular diterpene metabolism in nonmodel systems. Plant Physiol. 162 (2013) 1073–1091. [DOI] [PMID: 23613273] |
2. |
Pateraki, I., Andersen-Ranberg, J., Hamberger, B., Heskes, A.M., Martens, H.J., Zerbe, P., Bach, S.S., Moller, B.L., Bohlmann, J. and Hamberger, B. Manoyl oxide (13R), the biosynthetic precursor of forskolin, is synthesized in specialized root cork cells in Coleus forskohlii. Plant Physiol. 164 (2014) 1222–1236. [DOI] [PMID: 24481136] |
3. |
Zerbe, P., Chiang, A., Dullat, H., O'Neil-Johnson, M., Starks, C., Hamberger, B. and Bohlmann, J. Diterpene synthases of the biosynthetic system of medicinally active diterpenoids in Marrubium vulgare. Plant J. 79 (2014) 914–927. [DOI] [PMID: 24990389] |
|
[EC 4.2.3.190 created 2017] |
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|
|
|
EC |
4.2.3.220 | Relevance: 94.8% |
Accepted name: |
talaropentaene synthase |
Reaction: |
all-trans-hexaprenyl diphosphate = talaropentaene + diphosphate |
Glossary: |
talaropentaene = (3aS,5E,9E)-3a,6,10-trimethyl-1-[(2ξ,4E,8E)-undeca-5,9-dien-2-yl]-3,3a,4,7,8,11,12-octahydrocyclopenta[11]annulene |
Other name(s): |
TvTS |
Systematic name: |
pentaprenyl-diphosphate diphosphate-lyase [cyclizing, talaropentaene-forming] |
Comments: |
Isolated from the fungus Talaromyces verruculosus. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Tao, H., Lauterbach, L., Bian, G., Chen, R., Hou, A., Mori, T., Cheng, S., Hu, B., Lu, L., Mu, X., Li, M., Adachi, N., Kawasaki, M., Moriya, T., Senda, T., Wang, X., Deng, Z., Abe, I., Dickschat, J.S. and Liu, T. Discovery of non-squalene triterpenes. Nature 606 (2022) 414–419. [DOI] [PMID: 35650436] |
|
[EC 4.2.3.220 created 2024] |
|
|
|
|
EC |
4.2.3.27 | Relevance: 94.7% |
Accepted name: |
isoprene synthase |
Reaction: |
prenyl diphosphate = isoprene + diphosphate |
|
For diagram of isoprene biosynthesis and metabolism, click here |
Glossary: |
isoprene = 2-methylbuta-1,3-diene |
Other name(s): |
ISPC; ISPS; dimethylallyl-diphosphate diphosphate-lyase (isoprene-forming) |
Systematic name: |
prenyl-diphosphate diphosphate-lyase (isoprene-forming) |
Comments: |
Requires Mg2+ or Mn2+ for activity. This enzyme is located in the chloroplast of isoprene-emitting plants, such as poplar and aspen, and may be activitated by light-dependent changes in chloroplast pH and Mg2+ concentration [2,8]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 139172-14-8 |
References: |
1. |
Silver, G.M. and Fall, R. Enzymatic synthesis of isoprene from dimethylallyl diphosphate in aspen leaf extracts. Plant Physiol. 97 (1991) 1588–1591. [PMID: 16668590] |
2. |
Silver, G.M. and Fall, R. Characterization of aspen isoprene synthase, an enzyme responsible for leaf isoprene emission to the atmosphere. J. Biol. Chem. 270 (1995) 13010–13016. [DOI] [PMID: 7768893] |
3. |
Wildermuth, M.C. and Fall, R. Light-dependent isoprene emission (characterization of a thylakoid-bound isoprene synthase in Salix discolor chloroplasts). Plant Physiol. 112 (1996) 171–182. [PMID: 12226383] |
4. |
Schnitzler, J.P., Arenz, R., Steinbrecher, R. and Lehming, A. Characterization of an isoprene synthase from leaves of Quercus petraea. Bot. Acta 109 (1996) 216–221. |
5. |
Miller, B., Oschinski, C. and Zimmer, W. First isolation of an isoprene synthase gene from poplar and successful expression of the gene in Escherichia coli. Planta 213 (2001) 483–487. [PMID: 11506373] |
6. |
Sivy, T.L., Shirk, M.C. and Fall, R. Isoprene synthase activity parallels fluctuations of isoprene release during growth of Bacillus subtilis. Biochem. Biophys. Res. Commun. 294 (2002) 71–75. [DOI] [PMID: 12054742] |
7. |
Sasaki, K., Ohara, K. and Yazaki, K. Gene expression and characterization of isoprene synthase from Populus alba. FEBS Lett. 579 (2005) 2514–2518. [DOI] [PMID: 15848197] |
8. |
Schnitzler, J.-P., Zimmer, I., Bachl, A., Arend, M., Fromm, J. and Fischbach, R.J. Biochemical properties of isoprene synthase in poplar (Populus x canescens). Planta 222 (2005) 777–786. [DOI] [PMID: 16052321] |
|
[EC 4.2.3.27 created 2007] |
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|
|
|
EC |
4.2.3.63 | Relevance: 94.2% |
Accepted name: |
(+)-cubenene synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = (+)-cubenene + diphosphate |
|
For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-cubenene-forming] |
Comments: |
Requires Mg2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Nabeta, K., Kigure, K., Fujita, M., Nagoya, T., Ishikawa, T., Okuyama, H. and Takasawa, T. Bioynthesis of (+)-cubenene and (+)-epicubenol by cell-free extracts of cultured cells of Heteroscyphus planus and cyclization of [2H]farnesyl diphosphates. J. Chem. Soc., Perkin Trans. 1 (1995) 1935–1939. |
2. |
Nabeta, K., Fujita, M., Komuro, K., Katayama, K., and Takasawa, T. In vitro biosynthesis of cadinanes by cell-free extracts of cultured cells of Heteroscyphus planus. J. Chem. Soc., Perkin Trans. 1 (1997) 2065–2070. |
|
[EC 4.2.3.63 created 2011] |
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|
|
|
EC |
2.5.1.103 | Relevance: 94.1% |
Accepted name: |
presqualene diphosphate synthase |
Reaction: |
2 (2E,6E)-farnesyl diphosphate = presqualene diphosphate + diphosphate |
|
For diagram of botryococcus braunii BOT22 squalene and botrycoccene biosynthesis, click here |
Other name(s): |
SSL-1 (gene name); hpnD (gene name) |
Systematic name: |
(2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate-forming) |
Comments: |
Isolated from the green alga Botryococcus braunii BOT22. Unlike EC 2.5.1.21, squalene synthase, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme. This compound is then converted into either squalene (by EC 1.3.1.96, Botryococcus squalene synthase) or botryococcene (EC 1.3.1.97, botryococcene synthase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Niehaus, T.D., Okada, S., Devarenne, T.P., Watt, D.S., Sviripa, V. and Chappell, J. Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii. Proc. Natl. Acad. Sci. USA 108 (2011) 12260–12265. [DOI] [PMID: 21746901] |
2. |
Pan, J.J., Solbiati, J.O., Ramamoorthy, G., Hillerich, B.S., Seidel, R.D., Cronan, J.E., Almo, S.C. and Poulter, C.D. Biosynthesis of squalene from farnesyl diphosphate in bacteria: three steps catalyzed by three enzymes. ACS Cent. Sci. 1 (2015) 77–82. [DOI] [PMID: 26258173] |
|
[EC 2.5.1.103 created 2012] |
|
|
|
|
EC |
2.1.1.363 | Relevance: 94.1% |
Accepted name: |
pre-sodorifen synthase |
Reaction: |
S-adenosyl-L-methionine + (2E,6E)-farnesyl diphosphate = S-adenosyl-L-homocysteine + pre-sodorifen diphosphate |
Glossary: |
pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
sodorifen = (1S,2S,4R,5S,8s)-1,2,4,5,6,7,8-heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene |
Other name(s): |
sodC (gene name) |
Systematic name: |
(2E,6E)-farnesyl diphosphate 10-C-methyltransferase (cyclyzing, pre-sodorifen diphosphate producing) |
Comments: |
The enzyme, characterized from the bacterium Serratia plymuthica, participates in biosynthesis of sodorifen. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14): fnw139 (2016). [DOI] [PMID: 27231241] |
2. |
Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci. Rep. 7:862 (2017). [PMID: 28408760] |
3. |
von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855–11862. [PMID: 30133268] |
|
[EC 2.1.1.363 created 2019] |
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|
|
|
EC |
4.2.3.97 | Relevance: 94% |
Accepted name: |
(-)-δ-cadinene synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = (-)-δ-cadinene + diphosphate |
|
For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here |
Glossary: |
(-)-δ-cadinene = (1R,8aS)-4,7-dimethyl-1-(propan-2-yl)-1,2,3,5,6,8a-hexahydronaphthalene |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (-)-δ-cadinene-forming) |
Comments: |
The cyclization mechanism involves an intermediate nerolidyl diphosphate leading to a helminthogermacradienyl cation. Following a 1,3-hydride shift of the original 1-pro-S hydrogen of (2E,6E)-farnesyl diphosphate, cyclization and deprotonation gives (-)-δ-cadinene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hu, Y., Chou, W.K., Hopson, R. and Cane, D.E. Genome mining in Streptomyces clavuligerus: expression and biochemical characterization of two new cryptic sesquiterpene synthases. Chem. Biol. 18 (2011) 32–37. [DOI] [PMID: 21276937] |
|
[EC 4.2.3.97 created 2012] |
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|
|
|
EC |
2.5.1.20 | Relevance: 93.8% |
Accepted name: |
rubber cis-polyprenylcistransferase |
Reaction: |
polycis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit |
|
For diagram of all-cis-polyprenyl diphosphate, click here |
Other name(s): |
rubber allyltransferase; rubber transferase; isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase; cis-prenyl transferase; rubber polymerase; rubber prenyltransferase |
Systematic name: |
polycis-polyprenyl-diphosphate:isopentenyl-diphosphate polyprenylcistransferase |
Comments: |
Rubber particles act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-41-6 |
References: |
1. |
Archer, B.L. and Cockbain, E.G. Rubber transferase from Hevea brasiliensis latex. Methods Enzymol. 15 (1969) 476–480. |
2. |
McMullen, A.I. and McSweeney, G.P. The biosynthesis of rubber. Incorporation of isopentenyl pyrophosphate into purified rubber particles by a soluble latex-serum enzyme. Biochem. J. 101 (1966) 42–47. [PMID: 16742418] |
|
[EC 2.5.1.20 created 1976] |
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|
|
EC |
4.2.3.131 | Relevance: 93.7% |
Accepted name: |
miltiradiene synthase |
Reaction: |
(+)-copalyl diphosphate = miltiradiene + diphosphate |
|
For diagram of abietane diterpenoids biosynthesis, click here |
Other name(s): |
SmMDS; SmiKSL; RoKSL |
Systematic name: |
(+)-copalyl-diphosphate diphosphate-lyase (cyclizing, miltiradiene-forming) |
Comments: |
Isolated from the plants Rosmarinus officinalis (rosemary) and Salvia miltiorrhiza. The enzyme from the plant Selaginella moellendorffii is mutifunctional and also catalyses EC 5.5.1.12, copalyl diphosphate synthase [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gao, W., Hillwig, M.L., Huang, L., Cui, G., Wang, X., Kong, J., Yang, B. and Peters, R.J. A functional genomics approach to tanshinone biosynthesis provides stereochemical insights. Org. Lett. 11 (2009) 5170–5173. [DOI] [PMID: 19905026] |
2. |
Sugai, Y., Ueno, Y., Hayashi, K., Oogami, S., Toyomasu, T., Matsumoto, S., Natsume, M., Nozaki, H. and Kawaide, H. Enzymatic 13C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii. J. Biol. Chem. 286 (2011) 42840–42847. [DOI] [PMID: 22027823] |
3. |
Bruckner, K., Bozic, D., Manzano, D., Papaefthimiou, D., Pateraki, I., Scheler, U., Ferrer, A., de Vos, R.C., Kanellis, A.K. and Tissier, A. Characterization of two genes for the biosynthesis of abietane-type diterpenes in rosemary (Rosmarinus officinalis) glandular trichomes. Phytochemistry 101 (2014) 52–64. [DOI] [PMID: 24569175] |
|
[EC 4.2.3.131 created 2012] |
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|
|
EC |
2.5.1.1 | Relevance: 93.7% |
Accepted name: |
dimethylallyltranstransferase |
Reaction: |
prenyl diphosphate + 3-methylbut-3-en-1-yl diphosphate = diphosphate + geranyl diphosphate |
|
For diagram of terpenoid biosynthesis, click here |
Glossary: |
3-methylbut-3-en-1-yl = isopentenyl (ambiguous)
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl (ambiguous) |
Other name(s): |
geranyl-diphosphate synthase; prenyltransferase; dimethylallyltransferase; DMAPP:IPP-dimethylallyltransferase; (2E,6E)-farnesyl diphosphate synthetase; diprenyltransferase; geranyl pyrophosphate synthase; geranyl pyrophosphate synthetase; trans-farnesyl pyrophosphate synthetase; dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallyltranstransferase |
Systematic name: |
prenyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate prenyltranstransferase |
Comments: |
This enzyme will not accept larger prenyl diphosphates as efficient donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-79-5 |
References: |
1. |
Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91–100. |
2. |
Sagami, H., Ogura, K., Seto, S. and Kurokawa, T. A new prenyltransferase from Micrococcus lysodeikticus. Biochem. Biophys. Res. Commun. 85 (1978) 572–578. [DOI] [PMID: 736921] |
|
[EC 2.5.1.1 created 1961] |
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|
|
|
EC |
4.2.3.213 | Relevance: 93.5% |
Accepted name: |
colleterpenol synthase |
Reaction: |
all-trans-hexaprenyl diphosphate + H2O = colleterpenol + diphosphate
|
Glossary: |
colleterpenol = (2S)-2-[(1R,3E,7E,11E)-4,8,12-trimethylcyclotetradeca-3,7,11-trien-1-yl]undeca-5,9-dien-2-ol |
Other name(s): |
CgCS |
Systematic name: |
pentaprenyl-diphosphate diphosphate-lyase [cyclizing, colleterpenol-forming] |
Comments: |
Isolated from Colletotrichum gloeosporioides, a pathogenic fungus that causes bitter rot in variety of crops. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Tao, H., Lauterbach, L., Bian, G., Chen, R., Hou, A., Mori, T., Cheng, S., Hu, B., Lu, L., Mu, X., Li, M., Adachi, N., Kawasaki, M., Moriya, T., Senda, T., Wang, X., Deng, Z., Abe, I., Dickschat, J.S. and Liu, T. Discovery of non-squalene triterpenes. Nature 606 (2022) 414–419. [DOI] [PMID: 35650436] |
|
[EC 4.2.3.213 created 2023] |
|
|
|
|
EC |
4.2.3.11 | Relevance: 93.2% |
Accepted name: |
sabinene-hydrate synthase |
Reaction: |
geranyl diphosphate + H2O = sabinene hydrate + diphosphate |
|
For diagram of monoterpenoid biosynthesis, click here |
Other name(s): |
sabinene hydrate cyclase |
Systematic name: |
geranyl-diphosphate diphosphate-lyase (cyclizing, sabinene-hydrate-forming) |
Comments: |
Both cis- and trans- isomers of sabinene hydrate are formed. (3R)-Linalyl diphosphate is an intermediate in the reaction |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117164-95-1 |
References: |
1. |
Hallahan, T.W. and Croteau, R. Monoterpene biosynthesis: demonstration of a geranyl pyrophosphate:sabinene hydrate cyclase in soluble enzyme preparations from sweet marjoram (Majorana hortensis). Arch. Biochem. Biophys. 264 (1988) 618–631. [DOI] [PMID: 3401015] |
2. |
Hallahan, T.W. and Croteau, R. Monoterpene biosynthesis: mechanism and stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and (+)-trans-sabinene hydrate. Arch. Biochem. Biophys. 269 (1989) 313–326. [DOI] [PMID: 2916845] |
|
[EC 4.2.3.11 created 1992 as EC 4.6.1.9, transferred 2000 to EC 4.2.3.11] |
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|
|
|
EC |
4.2.3.115 | Relevance: 93.1% |
Accepted name: |
α-terpinene synthase |
Reaction: |
geranyl diphosphate = α-terpinene + diphosphate |
|
For diagram of menthane monoterpenoid biosynthesis, click here |
Glossary: |
α-terpinene = 1-isopropyl-4-methylcyclohexa-1,3-diene |
Systematic name: |
geranyl-diphosphate diphosphate-lyase (cyclizing, α-terpinene-forming) |
Comments: |
The enzyme has been characterized from Dysphania ambrosioides (American wormseed). Requires Mg2+. Mn2+ is less effective. The enzyme will also use (3R)-linalyl diphosphate. The reaction involves a 1,2-hydride shift. The 1-pro-S hydrogen of geranyl diphosphate is lost. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Poulose, A.J. and Croteau, R. γ-Terpinene synthetase: a key enzyme in the biosynthesis of aromatic monoterpenes. Arch. Biochem. Biophys. 191 (1978) 400–411. [DOI] [PMID: 736574] |
2. |
LaFever, R.E. and Croteau, R. Hydride shifts in the biosynthesis of the p-menthane monoterpenes α-terpinene, γ-terpinene, and β-phellandrene. Arch. Biochem. Biophys. 301 (1993) 361–366. [DOI] [PMID: 8460944] |
|
[EC 4.2.3.115 created 2012] |
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|
EC |
4.2.3.145 | Relevance: 93.1% |
Accepted name: |
ophiobolin F synthase |
Reaction: |
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + H2O = ophiobolin F + diphosphate |
|
For diagram of biosynthesis of diterpenoids from ent-copalyl diphosphate, click here and for diagram of sesterterpenoids biosynthesis, click here |
Systematic name: |
(2E,6E,10E,14E)-geranylfarnesyl-diphosphate diphosphate-lyase (cyclizing, ophiobolin-F-forming) |
Comments: |
Isolated from the fungus Aspergillus clavatus. The product is a sesterterpenoid (C25 terpenoid). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chiba, R., Minami, A., Gomi, K. and Oikawa, H. Identification of ophiobolin F synthase by a genome mining approach: a sesterterpene synthase from Aspergillus clavatus. Org. Lett. 15 (2013) 594–597. [DOI] [PMID: 23324037] |
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[EC 4.2.3.145 created 2014] |
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EC |
4.2.3.34 | Relevance: 93.1% |
Accepted name: |
stemod-13(17)-ene synthase |
Reaction: |
9α-copalyl diphosphate = stemod-13(17)-ene + diphosphate |
|
For diagram of the biosynthesis of diterpenoids from 9alpha-copalyl diphosphate, click here |
Glossary: |
syn-copalyl diphosphate = 9α-copalyl diphosphate
exo-stemodene = stemod-13(17)-ene |
Other name(s): |
OsKSL11; stemodene synthase |
Systematic name: |
9α-copalyl-diphosphate diphosphate-lyase [stemod-13(17)-ene-forming] |
Comments: |
This enzyme catalyses the committed step in the biosynthesis of the stemodane family of diterpenoid secondary metabolites, some of which possess mild antiviral activity. The enzyme also produces stemod-12-ene and stemar-13-ene as minor products. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Morrone, D., Jin, Y., Xu, M., Choi, S.Y., Coates, R.M. and Peters, R.J. An unexpected diterpene cyclase from rice: functional identification of a stemodene synthase. Arch. Biochem. Biophys. 448 (2006) 133–140. [DOI] [PMID: 16256063] |
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[EC 4.2.3.34 created 2008] |
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EC |
5.5.1.13 | Relevance: 93.1% |
Accepted name: |
ent-copalyl diphosphate synthase |
Reaction: |
geranylgeranyl diphosphate = ent-copalyl diphosphate |
|
For diagram of biosynthesis of diterpenoids from ent-copalyl diphosphate, click here |
Other name(s): |
ent-kaurene synthase A; ent-kaurene synthetase A; ent-CDP synthase; ent-copalyl-diphosphate lyase (decyclizing) |
Systematic name: |
ent-copalyl-diphosphate lyase (ring-opening) |
Comments: |
Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9055-64-5 |
References: |
1. |
Fall, R.R., West, C.A. Purification and properties of kaurene synthetase from Fusarium moniliforme. J. Biol. Chem. 246 (1971) 6913–6928. [PMID: 4331199] |
2. |
Sun, T.P. and Kamiya, Y. The Arabidopsis GA1 locus encodes the cyclase ent-kaurene synthetase A of gibberellin biosynthesis. Plant Cell 6 (1994) 1509–1518. [PMID: 7994182] |
3. |
Kawaide, H., Imai, R., Sassa, T. and Kamiya, Y. Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis. J. Biol. Chem. 272 (1997) 21706–21712. [DOI] [PMID: 9268298] |
4. |
Toyomasu, T., Kawaide, H., Ishizaki, A., Shinoda, S., Otsuka, M., Mitsuhashi, W. and Sassa, T. Cloning of a full-length cDNA encoding ent-kaurene synthase from Gibberella fujikuroi: functional analysis of a bifunctional diterpene cyclase. Biosci. Biotechnol. Biochem. 64 (2000) 660–664. [DOI] [PMID: 10803977] |
|
[EC 5.5.1.13 created 2002] |
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EC |
2.5.1.112 | Relevance: 93% |
Accepted name: |
adenylate dimethylallyltransferase (ADP/ATP-dependent) |
Reaction: |
(1) prenyl diphosphate + ADP = diphosphate + N6-prenyladenosine 5′-diphosphate (2) prenyl diphosphate + ATP = diphosphate + N6-prenyladenosine 5′-triphosphate |
|
For diagram of N6-(Dimethylallyl)adenosine phosphates biosynthesis, click here |
Other name(s): |
cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:ADP/ATP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); dimethylallyl diphosphate:ATP/ADP isopentenyltransferase: IPT; dimethylallyl-diphosphate:ADP/ATP dimethylallyltransferase |
Systematic name: |
prenyl-diphosphate:ADP/ATP prenyltransferase |
Comments: |
Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP [1]. Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus [3], also have a lower activity with AMP (cf. EC 2.5.1.27, adenylate dimethylallyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kakimoto, T. Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate:ATP/ADP isopentenyltransferases. Plant Cell Physiol. 42 (2001) 677–685. [PMID: 11479373] |
2. |
Takei, K., Sakakibara, H. and Sugiyama, T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 26405–26410. [DOI] [PMID: 11313355] |
3. |
Sakano, Y., Okada, Y., Matsunaga, A., Suwama, T., Kaneko, T., Ito, K., Noguchi, H. and Abe, I. Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.). Phytochemistry 65 (2004) 2439–2446. [DOI] [PMID: 15381407] |
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[EC 2.5.1.112 created 2013] |
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EC |
4.2.3.25 | Relevance: 93% |
Accepted name: |
S-linalool synthase |
Reaction: |
geranyl diphosphate + H2O = (3S)-linalool + diphosphate |
|
For diagram of acyclic monoterpenoid biosynthesis, click here |
Glossary: |
(3S)-linalool = (3S)-3,7-dimethylocta-1,6-dien-3-ol |
Other name(s): |
LIS; Lis; 3S-linalool synthase |
Systematic name: |
geranyl-diphosphate diphosphate-lyase [(3S)-linalool-forming] |
Comments: |
Requires Mn2+ or Mg2+ for activity. Neither (S)- nor (R)-linalyl diphosphate can act as substrate for the enzyme from the flower Clarkia breweri [1]. Unlike many other monoterpene synthases, only a single product, (3S)-linalool, is formed. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 160477-81-6 |
References: |
1. |
Pichersky, E., Lewinsohn, E. and Croteau, R. Purification and characterization of S-linalool synthase, an enzyme
involved in the production of floral scent in Clarkia breweri. Arch. Biochem. Biophys. 316 (1995) 803–807. [DOI] [PMID: 7864636] |
2. |
Lücker, J., Bouwmeester, H.J., Schwab, W., Blaas, J., van der Plas, L.H. and Verhoeven, H.A. Expression of Clarkia S-linalool synthase in transgenic petunia plants results in the accumulation of S-linalyl-β-D-glucopyranoside. Plant J. 27 (2001) 315–324. [DOI] [PMID: 11532177] |
3. |
Dudareva, N., Cseke, L., Blanc, V.M. and Pichersky, E. Evolution of floral scent in Clarkia: novel patterns of S-linalool synthase gene expression in the C. breweri flower. Plant Cell 8 (1996) 1137–1148. [DOI] [PMID: 8768373] |
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[EC 4.2.3.25 created 2006] |
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EC |
4.2.3.37 | Relevance: 92.9% |
Accepted name: |
epi-isozizaene synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene + diphosphate |
|
|
Other name(s): |
SCO5222 protein |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-epi-isozizaene-forming] |
Comments: |
Requires Mg2+ for activity. The displacement of the diphosphate group of farnesyl diphosphate occurs with retention of configuration [1]. In the soil-dwelling bacterium Streptomyces coelicolor A3(2), the product of this reaction is used by EC 1.14.13.106, epi-isozizaene 5-monooxygenase, to produce the sesquiterpene antibiotic albaflavenone [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Lin, X., Hopson, R. and Cane, D.E. Genome mining in Streptomyces coelicolor: molecular cloning and characterization of a new sesquiterpene synthase. J. Am. Chem. Soc. 128 (2006) 6022–6023. [DOI] [PMID: 16669656] |
2. |
Zhao, B., Lin, X., Lei, L., Lamb, D.C., Kelly, S.L., Waterman, M.R. and Cane, D.E. Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2). J. Biol. Chem. 283 (2008) 8183–8189. [DOI] [PMID: 18234666] |
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[EC 4.2.3.37 created 2008] |
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EC |
3.1.7.5 | Relevance: 92.8% |
Accepted name: |
geranylgeranyl diphosphate diphosphatase |
Reaction: |
geranylgeranyl diphosphate + H2O = geranylgeraniol + diphosphate |
|
For diagram of acyclic diterpenoid biosynthesis, click here |
Glossary: |
plaunotol = 18-hydroxygeranylgeraniol |
Other name(s): |
geranylgeranyl diphosphate phosphatase |
Systematic name: |
geranyl-diphosphate diphosphohydrolase |
Comments: |
Involved in the biosynthesis of plaunotol. There are two isoenzymes with different ion requirements. Neither require Mg2+ but in addition PII is inhibited by Zn2+, Mn2+ and Co2+. It is not known which isoenzyme is involved in plaunotol biosynthesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Nualkaew, N., De-Eknamkul, W., Kutchan, T.M. and Zenk, M.H. Membrane-bound geranylgeranyl diphosphate phosphatases: purification and characterization from Croton stellatopilosus leaves. Phytochemistry 67 (2006) 1613–1620. [DOI] [PMID: 16445953] |
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[EC 3.1.7.5 created 2009] |
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EC |
4.2.3.205 | Relevance: 92.7% |
Accepted name: |
sodorifen synthase |
Reaction: |
pre-sodorifen diphosphate = sodorifen + diphosphate |
Glossary: |
pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
sodorifen = (1S,2R,8S)-1,2,4,5,6,7,8-Heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene |
Other name(s): |
sodD (gene name) |
Systematic name: |
pre-sodorifen diphosphate-lyase [sodorifen-forming] |
Comments: |
The enzyme has been characterized from the bacterium Serratia plymuthica. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14): fnw139 (2016). [DOI] [PMID: 27231241] |
2. |
Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci. Rep. 7:862 (2017). [PMID: 28408760] |
3. |
von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855–11862. [PMID: 30133268] |
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[EC 4.2.3.205 created 2019] |
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EC |
4.2.3.71 | Relevance: 92.6% |
Accepted name: |
(E,E)-germacrene B synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = (E,E)-germacrene B + diphosphate |
|
For diagram of germacrene-derived sesquiterpenoid biosynthesis, click here |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(E,E)-germacrene-B-forming] |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
van Der Hoeven, R.S., Monforte, A.J., Breeden, D., Tanksley, S.D. and Steffens, J.C. Genetic control and evolution of sesquiterpene biosynthesis in Lycopersicon esculentum and L. hirsutum. Plant Cell 12 (2000) 2283–2294. [PMID: 11090225] |
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[EC 4.2.3.71 created 2011] |
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EC |
4.2.3.60 | Relevance: 92.6% |
Accepted name: |
germacrene C synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = germacrene C + diphosphate |
|
For diagram of germacrene-derived sesquiterpenoid biosynthesis, click here |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (germacrene-C-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Colby, S.M., Crock, J., Dowdle-Rizzo, B., Lemaux, P.G. and Croteau, R. Germacrene C synthase from Lycopersicon esculentum cv. VFNT cherry tomato: cDNA isolation, characterization, and bacterial expression of the multiple product sesquiterpene cyclase. Proc. Natl. Acad. Sci. USA 95 (1998) 2216–2221. [DOI] [PMID: 9482865] |
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[EC 4.2.3.60 created 2011] |
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EC |
4.2.3.169 | Relevance: 92.5% |
Accepted name: |
7-epi-α-eudesmol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = 7-epi-α-eudesmol + diphosphate |
|
For diagram of eudesmol and selinene biosynthesis, click here |
Glossary: |
7-epi-α-eudesmol = 2-[(2S,4aR,8aR)-4a,8-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalen-2-yl]propan-2-ol |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, 7-epi-α-eudesmol-forming) |
Comments: |
The enzyme, found in the bacterium Streptomyces viridochromogenes, is specific for (2E,6E)-farnesyl diphosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rabe, P., Schmitz, T. and Dickschat, J.S. Mechanistic investigations on six bacterial terpene cyclases. Beilstein J. Org. Chem. 12 (2016) 1839–1850. [DOI] [PMID: 27829890] |
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[EC 4.2.3.169 created 2017] |
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EC |
4.2.3.166 | Relevance: 92.3% |
Accepted name: |
(+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol + diphosphate |
|
For diagram of biosynthesis of ent-germacrene sesquiterpenoids, click here |
Glossary: |
(+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol = (1S,2E,6E,10R)-3,7-dimethyl-10-(propan-2-yl)cyclodeca-2,6-dien-1-ol |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [cyclizing, (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol-forming] |
Comments: |
The enzyme has been identified in the bacterium Streptomyces pratensis. It is specific for (2E,6E)-farnesyl diphosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rabe, P., Barra, L., Rinkel, J., Riclea, R., Citron, C.A., Klapschinski, T.A., Janusko, A. and Dickschat, J.S. Conformational analysis, thermal rearrangement, and EI-MS fragmentation mechanism of ((1(10)E,4E,6S,7R)-germacradien-6-ol by 13C-labeling experiments. Angew. Chem. Int. Ed. Engl. 54 (2015) 13448–13451. [DOI] [PMID: 26361082] |
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[EC 4.2.3.166 created 2017] |
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EC |
1.23.1.3 | Relevance: 92.1% |
Accepted name: |
(–)-pinoresinol reductase |
Reaction: |
(–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+ |
|
For diagram of (–)-lariciresinol biosynthesis, click here |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 18347017] |
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[EC 1.23.1.3 created 2013] |
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EC
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3.1.7.8
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Transferred entry: | tuberculosinol synthase. Now known to be partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase.
|
[EC 3.1.7.8 created 2011, deleted 2020] |
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EC |
2.5.1.153 | Relevance: 92% |
Accepted name: |
adenosine tuberculosinyltransferase |
Reaction: |
tuberculosinyl diphosphate + adenosine = 1-tuberculosinyladenosine + diphosphate |
Glossary: |
tuberculosinyl diphosphate = halima-5,13-dien-15-yl diphosphate |
Other name(s): |
Rv3378c (locus name) |
Systematic name: |
tuberculosinyl-diphosphate:adenosine tuberculosinyltransferase |
Comments: |
The enzyme, characterized from the bacterial pathogen Mycobacterium tuberculosis, produces 1-tuberculosinyladenosine, an unusual terpene nucleoside that acts as a phagolysosome disruptor by neutralizing the pH, resulting in swelling of the lysosome and obliteration of its multilamellar structure. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Layre, E., Lee, H.J., Young, D.C., Martinot, A.J., Buter, J., Minnaard, A.J., Annand, J.W., Fortune, S.M., Snider, B.B., Matsunaga, I., Rubin, E.J., Alber, T. and Moody, D.B. Molecular profiling of Mycobacterium tuberculosis identifies tuberculosinyl nucleoside products of the virulence-associated enzyme Rv3378c. Proc. Natl. Acad. Sci. USA 111 (2014) 2978–2983. [DOI] [PMID: 24516143] |
2. |
Young, D.C., Layre, E., Pan, S.J., Tapley, A., Adamson, J., Seshadri, C., Wu, Z., Buter, J., Minnaard, A.J., Coscolla, M., Gagneux, S., Copin, R., Ernst, J.D., Bishai, W.R., Snider, B.B. and Moody, D.B. In vivo biosynthesis of terpene nucleosides provides unique chemical markers of Mycobacterium tuberculosis infection. Chem. Biol. 22 (2015) 516–526. [DOI] [PMID: 25910243] |
3. |
Buter, J., Cheng, T.Y., Ghanem, M., Grootemaat, A.E., Raman, S., Feng, X., Plantijn, A.R., Ennis, T., Wang, J., Cotton, R.N., Layre, E., Ramnarine, A.K., Mayfield, J.A., Young, D.C., Jezek Martinot, A., Siddiqi, N., Wakabayashi, S., Botella, H., Calderon, R., Murray, M., Ehrt, S., Snider, B.B., Reed, M.B., Oldfield, E., Tan, S., Rubin, E.J., Behr, M.A., van der Wel, N.N., Minnaard, A.J. and Moody, D.B. Mycobacterium tuberculosis releases an antacid that remodels phagosomes. Nat. Chem. Biol. 15 (2019) 889–899. [DOI] [PMID: 31427817] |
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[EC 2.5.1.153 created 2011 as EC 3.1.7.8 and EC 3.1.7.9, transferred 2020 to EC 2.5.1.153] |
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EC |
4.2.3.108 | Relevance: 91.9% |
Accepted name: |
1,8-cineole synthase |
Reaction: |
geranyl diphosphate + H2O = 1,8-cineole + diphosphate |
|
For diagram of menthane monoterpenoid biosynthesis, click here |
Glossary: |
1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane |
Other name(s): |
1,8-cineole cyclase; geranyl pyrophoshate:1,8-cineole cyclase; 1,8-cineole synthetase |
Systematic name: |
geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming) |
Comments: |
Requires Mn2+ or Zn2+. Mg2+ is less effective than either. 1,8-Cineole is the main product from the enzyme with just traces of other monoterpenoids. The oxygen atom is derived from water. The reaction proceeds via linalyl diphosphate and α-terpineol, the stereochemistry of both depends on the organism. However neither intermediate can substitute for geranyl diphosphate. The reaction in Salvia officinalis (sage) proceeds via (–)-(3R)-linalyl diphosphate [1-3] while that in Arabidopsis (rock cress) proceeds via (+)-(3S)-linalyl diphosphate [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 110637-19-9 |
References: |
1. |
Croteau, R., Alonso, W.R., Koepp, A.E. and Johnson, M.A. Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase. Arch. Biochem. Biophys. 309 (1994) 184–192. [DOI] [PMID: 8117108] |
2. |
Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J. Biol. Chem. 273 (1998) 14891–14899. [DOI] [PMID: 9614092] |
3. |
Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [DOI] [PMID: 12941302] |
4. |
Chen, F., Ro, D.K., Petri, J., Gershenzon, J., Bohlmann, J., Pichersky, E. and Tholl, D. Characterization of a root-specific Arabidopsis terpene synthase responsible for the formation of the volatile monoterpene 1,8-cineole. Plant Physiol. 135 (2004) 1956–1966. [DOI] [PMID: 15299125] |
5. |
Keszei, A., Brubaker, C.L., Carter, R., Kollner, T., Degenhardt, J. and Foley, W.J. Functional and evolutionary relationships between terpene synthases from Australian Myrtaceae. Phytochemistry 71 (2010) 844–852. [DOI] [PMID: 20399476] |
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[EC 4.2.3.108 created 2012] |
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EC |
4.2.3.75 | Relevance: 91.9% |
Accepted name: |
(-)-germacrene D synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate |
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For diagram of gurjunene, patchoulol and selinene biosynthesis, click here |
Glossary: |
(-)-germacrene D = (1E,6E,8S)-1-methyl-5-methylidene-8-(propan-2-yl)cyclodeca-1,6-diene |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(-)-germacrene-D-forming] |
Comments: |
In Solidago canadensis the biosynthesis results in the pro-R hydrogen at C-1 of the farnesy diphosphate ending up at C-11 of the (-)-germacrene D [1]. With Streptomyces coelicolor the pro-S hydrogen at C-1 ends up at C-11 of the (-)-germacrene D [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schmidt, C.O., Bouwmeester, H.J., Franke, S. and König, W.A. Mechanisms of the biosynthesis of sesquiterpene enantiomers (+)- and (-)-germacrene D in Solidago canadensis. Chirality 11 (1999) 353–362. |
2. |
He, X. and Cane, D.E. Mechanism and stereochemistry of the germacradienol/germacrene D synthase of Streptomyces coelicolor A3(2). J. Am. Chem. Soc. 126 (2004) 2678–2679. [DOI] [PMID: 14995166] |
3. |
Lucker, J., Bowen, P. and Bohlmann, J. Vitis vinifera terpenoid cyclases: functional identification of two sesquiterpene synthase cDNAs encoding (+)-valencene synthase and (-)-germacrene D synthase and expression of mono- and sesquiterpene synthases in grapevine flowers and berries. Phytochemistry 65 (2004) 2649–2659. [DOI] [PMID: 15464152] |
4. |
Prosser, I., Altug, I.G., Phillips, A.L., Konig, W.A., Bouwmeester, H.J. and Beale, M.H. Enantiospecific (+)- and (-)-germacrene D synthases, cloned from goldenrod, reveal a functionally active variant of the universal isoprenoid-biosynthesis aspartate-rich motif. Arch. Biochem. Biophys. 432 (2004) 136–144. [DOI] [PMID: 15542052] |
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[EC 4.2.3.75 created 2011] |
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EC |
4.2.3.33 | Relevance: 91.7% |
Accepted name: |
stemar-13-ene synthase |
Reaction: |
9α-copalyl diphosphate = stemar-13-ene + diphosphate |
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For diagram of the biosynthesis of diterpenoids from 9alpha-copalyl diphosphate, click here |
Glossary: |
syn-copalyl diphosphate = 9α-copalyl diphosphate |
Other name(s): |
OsDTC2; OsK8; OsKL8; OsKS8; stemarene synthase; syn-stemar-13-ene synthase |
Systematic name: |
9α-copalyl-diphosphate diphosphate-lyase (stemar-13-ene-forming) |
Comments: |
This diterpene cyclase produces stemar-13-ene, a putative precursor of the rice phytoalexin oryzalexin S. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mohan, R.S., Yee, N.K., Coates, R.M., Ren, Y.Y., Stamenkovic, P., Mendez, I. and West, C.A. Biosynthesis of cyclic diterpene hydrocarbons in rice cell suspensions: conversion of 9,10-syn-labda-8(17),13-dienyl diphosphate to 9β-pimara-7,15-diene and stemar-13-ene. Arch. Biochem. Biophys. 330 (1996) 33–47. [DOI] [PMID: 8651702] |
2. |
Nemoto, T., Cho, E.M., Okada, A., Okada, K., Otomo, K., Kanno, Y., Toyomasu, T., Mitsuhashi, W., Sassa, T., Minami, E., Shibuya, N., Nishiyama, M., Nojiri, H. and Yamane, H. Stemar-13-ene synthase, a diterpene cyclase involved in the biosynthesis of the phytoalexin oryzalexin S in rice. FEBS Lett. 571 (2004) 182–186. [DOI] [PMID: 15280039] |
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[EC 4.2.3.33 created 2008] |
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