The Enzyme Database

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EC 4.2.3.18     
Accepted name: abieta-7,13-diene synthase
Reaction: (+)-copalyl diphosphate = abieta-7,13-diene + diphosphate
For diagram of abietadiene, abietate, isopimaradiene, phyllocladan-16alpha-ol and sclareol biosynthesis, click here and for diagram of reaction, click here
Glossary: (+)-copalyl diphosphate = (2E)-3-methyl-5-[(1S,4aS,8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]pent-2-en-1-yl trihydrogen diphosphate
abieta-7,13-diene = (4aS,4bR,10aS)-7-isopropyl-1,1,4a-trimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene
Other name(s): copalyl-diphosphate diphosphate-lyase (cyclizing) (ambiguous); abietadiene synthase (ambiguous)
Systematic name: (+)-copalyl-diphosphate diphosphate-lyase [cyclizing, abieta-7,13-diene-forming]
Comments: Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. See also EC 5.5.1.12, copalyl diphosphate synthase. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 157972-08-2
References:
1.  Peters, R.J., Flory, J.E., Jetter, R., Ravn, M.M., Lee, H.J., Coates, R.M. and Croteau, R.B. Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme. Biochemistry 39 (2000) 15592–15602. [DOI] [PMID: 11112547]
2.  Peters, R.J., Ravn, M.M., Coates, R.M. and Croteau, R.B. Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites. J. Am. Chem. Soc. 123 (2001) 8974–8978. [DOI] [PMID: 11552804]
3.  Peters, R.J. and Croteau, R.B. Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement. Proc. Natl. Acad. Sci. USA 99 (2002) 580–584. [DOI] [PMID: 11805316]
4.  Peters, R.J. and Croteau, R.B. Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate. Biochemistry 41 (2002) 1836–1842. [DOI] [PMID: 11827528]
5.  Ravn, M.M., Peters, R.J., Coates, R.M. and Croteau, R. Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates. J. Am. Chem. Soc. 124 (2002) 6998–7006. [DOI] [PMID: 12059223]
[EC 4.2.3.18 created 2002, modified 2012]
 
 
EC 4.2.3.32     
Accepted name: levopimaradiene synthase
Reaction: (+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here and for diagram of abietadiene, levopimaradiene and isopimara-7,15-diene biosynthesis, click here
Glossary: levopimaradiene = abieta-8(14),12-diene
Other name(s): PtTPS-LAS; LPS; copalyl-diphosphate diphosphate-lyase [abieta-8(14),12-diene-forming]
Systematic name: (+)-copalyl-diphosphate diphosphate-lyase [abieta-8(14),12-diene-forming]
Comments: In Ginkgo, the enzyme catalyses the initial cyclization step in the biosynthesis of ginkgolides, a structurally unique family of diterpenoids that are highly specific platelet-activating-factor receptor antagonists [1]. Levopimaradiene is widely distributed in higher plants. In some species the enzyme also forms abietadiene, palustradiene, and neoabietadiene [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schepmann, H.G., Pang, J. and Matsuda, S.P. Cloning and characterization of Ginkgo biloba levopimaradiene synthase which catalyzes the first committed step in ginkgolide biosynthesis. Arch. Biochem. Biophys. 392 (2001) 263–269. [DOI] [PMID: 11488601]
2.  Ro, D.K. and Bohlmann, J. Diterpene resin acid biosynthesis in loblolly pine (Pinus taeda): functional characterization of abietadiene/levopimaradiene synthase (PtTPS-LAS) cDNA and subcellular targeting of PtTPS-LAS and abietadienol/abietadienal oxidase (PtAO, CYP720B1). Phytochemistry 67 (2006) 1572–1578. [DOI] [PMID: 16497345]
[EC 4.2.3.32 created 2008, modified 2012]
 
 
EC 4.2.3.44     
Accepted name: isopimara-7,15-diene synthase
Reaction: (+)-copalyl diphosphate = isopimara-7,15-diene + diphosphate
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here and for diagram of abietadiene, levopimaradiene and isopimara-7,15-diene biosynthesis, click here
Glossary: isopimara-7,15-diene = 13α-pimara-7,15-diene
Other name(s): PaTPS-Iso; copalyl diphosphate-lyase (isopimara-7,15-diene-forming)
Systematic name: (+)-copalyl diphosphate-lyase (isopimara-7,15-diene-forming)
Comments: The enzyme only gave isopimara-7,15-diene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Martin, D.M., Faldt, J. and Bohlmann, J. Functional characterization of nine Norway Spruce TPS genes and evolution of gymnosperm terpene synthases of the TPS-d subfamily. Plant Physiol. 135 (2004) 1908–1927. [DOI] [PMID: 15310829]
[EC 4.2.3.44 created 2009]
 
 
EC 4.2.3.45     
Accepted name: phyllocladan-16α-ol synthase
Reaction: (+)-copalyl diphosphate + H2O = phyllocladan-16α-ol + diphosphate
For diagram of abietadiene, aphidicolanol, sclareol and terpentetriene biosynthesis, click here and for mechanism of reaction, click here
Other name(s): PaDC1
Systematic name: (+)-copalyl-diphosphate diphosphate-lyase (phyllocladan-16α-ol-forming)
Comments: The adjacent gene PaDC2 codes EC 5.5.1.12 copalyl diphosphate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Toyomasu, T., Niida, R., Kenmoku, H., Kanno, Y., Miura, S., Nakano, C., Shiono, Y., Mitsuhashi, W., Toshima, H., Oikawa, H., Hoshino, T., Dairi, T., Kato, N. and Sassa, T. Identification of diterpene biosynthetic gene clusters and functional analysis of labdane-related diterpene cyclases in Phomopsis amygdali. Biosci. Biotechnol. Biochem. 72 (2008) 1038–1047. [DOI] [PMID: 18391465]
[EC 4.2.3.45 created 2009]
 
 
EC 4.2.3.131     
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
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]
 
 
EC 4.2.3.132     
Accepted name: neoabietadiene synthase
Reaction: (+)-copalyl diphosphate = neoabietadiene + diphosphate
For diagram of abietane diterpenoids biosynthesis, click here
Glossary: neoabietadiene = abieta-8(14),13(15)-diene
Other name(s): TPS-LAS
Systematic name: (+)-copaly-diphosphate diphosphate-lyase (cyclizing, neoabietadiene-forming)
Comments: Isolated from Abies grandis (grand fir) [1]. This class I enzyme forms about equal proportions of abietadiene, levopimaradiene and neoabietadiene. See also EC 4.2.3.18, abieta-7,13-diene synthase and EC 4.2.3.32, levopimaradiene synthase. An X-ray study of this multifunctional enzyme showed that the class I activity is in the α domain, while (+)-copalyl diphosphate synthase activity (EC 5.5.1.12, a class II activity) is in the β and γ domains [2]. In Pinus taeda (loblolly pine) the major product is levopimaradiene, with less abietadiene and neoabietadiene [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Peters, R.J., Flory, J.E., Jetter, R., Ravn, M.M., Lee, H.J., Coates, R.M. and Croteau, R.B. Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme. Biochemistry 39 (2000) 15592–15602. [DOI] [PMID: 11112547]
2.  Zhou, K., Gao, Y., Hoy, J.A., Mann, F.M., Honzatko, R.B. and Peters, R.J. Insights into diterpene cyclization from structure of bifunctional abietadiene synthase from Abies grandis. J. Biol. Chem. 287 (2012) 6840–6850. [DOI] [PMID: 22219188]
3.  Ro, D.K. and Bohlmann, J. Diterpene resin acid biosynthesis in loblolly pine (Pinus taeda): functional characterization of abietadiene/levopimaradiene synthase (PtTPS-LAS) cDNA and subcellular targeting of PtTPS-LAS and abietadienol/abietadienal oxidase (PtAO, CYP720B1). Phytochemistry 67 (2006) 1572–1578. [DOI] [PMID: 16497345]
[EC 4.2.3.132 created 2012]
 
 
EC 4.2.3.147     
Accepted name: pimaradiene synthase
Reaction: (+)-copalyl diphosphate = pimara-8(14),15-diene + diphosphate
For diagram of pimarane diterpenoids biosynthesis, click here
Other name(s): PbmPIM1; PcmPIM1
Systematic name: (+)-copalyl diphosphate-lyase (pimara-8(14),15-diene-forming)
Comments: Isolated from the plants Pinus banksiana (jack pine) and Pinus contorta (lodgepole pine).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hall, D.E., Zerbe, P., Jancsik, S., Quesada, A.L., Dullat, H., Madilao, L.L., Yuen, M. and Bohlmann, J. Evolution of conifer diterpene synthases: diterpene resin acid biosynthesis in lodgepole pine and jack pine involves monofunctional and bifunctional diterpene synthases. Plant Physiol. 161 (2013) 600–616. [DOI] [PMID: 23370714]
[EC 4.2.3.147 created 2014]
 
 
EC 4.2.3.183     
Accepted name: nezukol synthase
Reaction: (+)-copalyl diphosphate + H2O = nezukol + diphosphate
For diagram of pimarane diterpenoids biosynthesis, click here
Glossary: (+)-copalyl diphosphate = (2E)-3-methyl-5-[(1S,4aS,8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]pent-2-en-1-yl trihydrogen diphosphate
nezukol = pimar-15-en-8-ol
Other name(s): TPS2
Systematic name: (+)-copalyl-diphosphate diphosphate-lyase (cyclizing, nezukol-forming)
Comments: Isolated from the plant Isodon rubescens.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pelot, K.A., Hagelthorn, D.M., Addison, J.B. and Zerbe, P. Biosynthesis of the oxygenated diterpene nezukol in the medicinal plant Isodon rubescens is catalyzed by a pair of diterpene synthases. PLoS One 12:e0176507 (2017). [DOI] [PMID: 28445526]
[EC 4.2.3.183 created 2017]
 
 
EC 4.2.3.193     
Accepted name: (12E)-labda-8(17),12,14-triene synthase
Reaction: (+)-copalyl diphosphate = (12E)-labda-8(17),12,14-triene + diphosphate
For diagram of pimarane diterpenoids biosynthesis, click here
Other name(s): CldD
Systematic name: (+)-copalyl-diphosphate diphosphate-lyase [(12E)-labda-8(17),12,14-triene-forming]
Comments: Isolated from the bacterium Streptomyces cyslabdanicus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamada, Y., Komatsu, M. and Ikeda, H. Chemical diversity of labdane-type bicyclic diterpene biosynthesis in Actinomycetales microorganisms. J. Antibiot. (Tokyo) 69 (2016) 515–523. [DOI] [PMID: 26814669]
[EC 4.2.3.193 created 2017]
 
 
EC 5.5.1.12     
Accepted name: copalyl diphosphate synthase
Reaction: geranylgeranyl diphosphate = (+)-copalyl diphosphate
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here, for diagram of labdane diterpenoids biosynthesis, click here and for diagram of pimarane diterpenoids biosynthesis, click here
Other name(s): (+)-copalyl-diphosphate lyase (decyclizing)
Systematic name: (+)-copalyl-diphosphate lyase (ring-opening)
Comments: In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. For example, in Selaginella moellendorffii this activity is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 157972-08-2
References:
1.  Peters, R.J., Ravn, M.M., Coates, R.M. and Croteau, R.B. Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites. J. Am. Chem. Soc. 123 (2001) 8974–8978. [DOI] [PMID: 11552804]
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.  Peters, R.J. and Croteau, R.B. Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement. Proc. Natl. Acad. Sci. USA 99 (2002) 580–584. [DOI] [PMID: 11805316]
4.  Ravn, M.M., Peters, R.J., Coates, R.M. and Croteau, R. Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates. J. Am. Chem. Soc. 124 (2002) 6998–7006. [DOI] [PMID: 12059223]
5.  Peters, R.J. and Croteau, R.B. Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate. Biochemistry 41 (2002) 1836–1842. [DOI] [PMID: 11827528]
[EC 5.5.1.12 created 2002, modified 2012]
 
 


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