The Enzyme Database

Displaying entries 51-100 of 127.

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EC 4.2.3.10     
Accepted name: (-)-endo-fenchol synthase
Reaction: geranyl diphosphate + H2O = (-)-endo-fenchol + diphosphate
For diagram of monoterpenoid biosynthesis, click here
Other name(s): (-)-endo-fenchol cyclase; geranyl pyrophosphate:(-)-endo-fenchol cyclase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-endo-fenchol-forming]
Comments: (3R)-Linalyl diphosphate is an intermediate in the reaction
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117758-41-5
References:
1.  Croteau, R., Miyazaki, J.H. and Wheeler, C.J. Monoterpene biosynthesis: mechanistic evaluation of the geranyl pyrophosphate:(-)-endo-fenchol cyclase from fennel (Foeniculum vulgare). Arch. Biochem. Biophys. 269 (1989) 507–516. [DOI] [PMID: 2919880]
2.  Croteau, R., Satterwhite, D.M., Wheeler, C.J. and Felton, N.M. Biosynthesis of monoterpenes. Stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (-)-endo-fenchol. J. Biol. Chem. 263 (1988) 15449–15453. [PMID: 3170591]
[EC 4.2.3.10 created 1992 as EC 4.6.1.8, transferred 2000 to EC 4.2.3.10]
 
 
EC 4.2.3.11     
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]
 
 
EC 4.2.3.14      
Deleted entry: pinene synthase. Now covered by EC 4.2.3.119, (-)-α-pinene synthase, and EC 4.2.3.120, (-)-β-pinene synthase
[EC 4.2.3.14 created 2000 as EC 4.1.99.8, transferred 2000 to EC 4.2.3.14, deleted 2012]
 
 
EC 4.2.3.15     
Accepted name: myrcene synthase
Reaction: geranyl diphosphate = myrcene + diphosphate
For diagram of monoterpenoid biosynthesis, click here
Glossary: myrcene = 7-methyl-3-methyleneocta-1,6-diene and is a monoterpenoid
Systematic name: geranyl-diphosphate diphosphate-lyase (myrcene-forming)
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 197462-59-2
References:
1.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [DOI] [PMID: 9268308]
[EC 4.2.3.15 created 2000 as EC 4.1.99.9, transferred 2000 to EC 4.2.3.15]
 
 
EC 4.2.3.16     
Accepted name: (4S)-limonene synthase
Reaction: geranyl diphosphate = (S)-limonene + diphosphate
For diagram of perillyl alcohol, isopiperitol and carveol biosynthesis, click here
Glossary: limonene = a monoterpenoid
(S)-limonene = (-)-limonene
Other name(s): (-)-(4S)-limonene synthase; 4S-(-)-limonene synthase; geranyldiphosphate diphosphate lyase (limonene forming); geranyldiphosphate diphosphate lyase [cyclizing, (4S)-limonene-forming]; geranyl-diphosphate diphosphate-lyase [cyclizing; (-)-(4S)-limonene-forming]
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing; (S)-limonene-forming]
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 110639-20-8
References:
1.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [DOI] [PMID: 9268308]
2.  Collby, S.M., Alonso, W.R., Katahira, E.J., McGarvey, D.J. and Croteau, R. 4S-Limonene synthase from the oil glands of spearmint (Mentha spicata). cDNA isolation, characterization, and bacterial expression of the catalytically active monoterpene cyclase. J. Biol. Chem. 268 (1993) 23016–23024. [PMID: 8226816]
3.  Yuba, A., Yazaki, K., Tabata, M., Honda, G. and Croteau, R. cDNA cloning, characterization, and functional expression of 4S-(-)-limonene synthase from Perilla frutescens. Arch. Biochem. Biophys. 332 (1996) 280–287. [DOI] [PMID: 8806736]
[EC 4.2.3.16 created 2000 as EC 4.1.99.10, transferred 2000 to EC 4.2.3.16, modified 2003]
 
 
EC 4.2.3.17     
Accepted name: taxadiene synthase
Reaction: geranylgeranyl diphosphate = taxa-4,11-diene + diphosphate
For diagram of taxadiene biosynthesis, click here
Other name(s): geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, taxadiene-forming)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cyclizing; taxa-4,11-diene-forming)
Comments: This is the committed step in the biosynthesis of the diterpenoid antineoplastic drug Taxol (paclitaxel). The cyclization involves a 1,5-hydride shift.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 169277-52-5
References:
1.  Koepp, A.E., Hezari, M., Zajicek, J., Vogel, B.S., LaFever, R.E., Lewis, N.G. and Croteau, R. Cyclization of geranylgeranyl diphosphate to taxa-4(5),11(12)-diene is the committed step of taxol biosynthesis in Pacific yew. J. Biol. Chem. 270 (1995) 8686–8690. [DOI] [PMID: 7721772]
2.  Hezari, M., Lewis, N.G. and Croteau, R. Purification and characterization of taxa-4(5),11(12)-diene synthase from Pacific yew (Taxus brevifolia) that catalyzes the first committed step of taxol biosynthesis. Arch. Biochem. Biophys. 322 (1995) 437–444. [DOI] [PMID: 7574719]
3.  Lin, X., Hezari, M., Koepp, A.E., Floss, H.G. and Croteau, R. Mechanism of taxadiene synthase, a diterpene cyclase that catalyzes the first step of taxol biosynthesis in Pacific yew. Biochemistry 35 (1996) 2968–2977. [DOI] [PMID: 8608134]
4.  Hezari, M., Ketchum, R.E., Gibson, D.M. and Croteau, R. Taxol production and taxadiene synthase activity in Taxus canadensis cell suspension cultures. Arch. Biochem. Biophys. 337 (1997) 185. [DOI] [PMID: 9016812]
5.  Williams, D.C., Carroll, B.J., Jin, Q., Rithner, C.D., Lenger, S.R., Floss, H.G., Coates, R.M., Williams, R.M. and Croteau, R. Intramolecular proton transfer in the cyclization of geranylgeranyl diphosphate to the taxadiene precursor of taxol catalyzed by recombinant taxadiene synthase. Chem. Biol. 7 (2000) 969–977. [DOI] [PMID: 11137819]
[EC 4.2.3.17 created 2002]
 
 
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, PDB, 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 4.2.3.20     
Accepted name: (R)-limonene synthase
Reaction: geranyl diphosphate = (R)-limonene + diphosphate
For diagram of carvone biosynthesis, click here
Glossary: (R)-limonene = (+)-limonene
Other name(s): (+)-limonene synthase; geranyldiphosphate diphosphate lyase [(+)-(R)-limonene-forming]; geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-(4R)-limonene-forming]
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (R)-limonene-forming]
Comments: Forms the first step of carvone biosynthesis in caraway. The enzyme from Carum carvi (caraway) seeds requires a divalent metal ion (preferably Mn2+) for catalysis. This enzyme occurs in Citrus, Carum (caraway) and Anethum (dill); (-)-limonene, however, is made in the fir, Abies, and mint, Mentha, by EC 4.2.3.16, (4S)-limonene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 155807-65-1
References:
1.  Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901–912. [PMID: 9662532]
2.  Lücker, J., El Tamer, M.K., Schwab, W., Verstappen, F.W., van der Plas, L.H., Bouwmeester, H.J. and Verhoeven, H.A. Monoterpene biosynthesis in lemon (Citrus limon). cDNA isolation and functional analysis of four monoterpene synthases. Eur. J. Biochem. 269 (2000) 3160–3171. [DOI] [PMID: 12084056]
3.  Maruyama, T., Ito, M., Kiuchi, F. and Honda, G. Molecular cloning, functional expression and characterization of d-limonene synthase from Schizonepeta tenuifolia. Biol. Pharm. Bull. 24 (2001) 373–377. [PMID: 11305598]
[EC 4.2.3.20 created 2003]
 
 
EC 4.2.3.24     
Accepted name: amorpha-4,11-diene synthase
Reaction: (2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
Other name(s): amorphadiene synthase
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (amorpha-4,11-diene-forming)
Comments: Requires Mg2+ and Mn2+ for activity. This is a key enzyme in the biosynthesis of the antimalarial endoperoxide artemisinin [3]. Catalyses the formation of both olefinic [e.g. amorpha-4,11-diene, amorpha-4,7(11)-diene, γ-humulene and β-sesquiphellandrene] and oxygenated (e.g. amorpha-4-en-7-ol) sesquiterpenes, with amorpha-4,11-diene being the major product. When geranyl diphosphate is used as a substrate, no monoterpenes are produced [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 259213-60-0
References:
1.  Wallaart, T.E., Bouwmeester, H.J., Hille, J., Poppinga, L. and Maijers, N.C. Amorpha-4,11-diene synthase: cloning and functional expression of a key enzyme in the biosynthetic pathway of the novel antimalarial drug artemisinin. Planta 212 (2001) 460–465. [DOI] [PMID: 11289612]
2.  Mercke, P., Bengtsson, M., Bouwmeester, H.J., Posthumus, M.A. and Brodelius, P.E. Molecular cloning, expression, and characterization of amorpha-4,11-diene synthase, a key enzyme of artemisinin biosynthesis in Artemisia annua L. Arch. Biochem. Biophys. 381 (2000) 173–180. [DOI] [PMID: 11032404]
3.  Bouwmeester, H.J., Wallaart, T.E., Janssen, M.H., van Loo, B., Jansen, B.J., Posthumus, M.A., Schmidt, C.O., De Kraker, J.W., König, W.A. and Franssen, M.C. Amorpha-4,11-diene synthase catalyses the first probable step in artemisinin biosynthesis. Phytochemistry 52 (1999) 843–854. [DOI] [PMID: 10626375]
4.  Chang, Y.J., Song, S.H., Park, S.H. and Kim, S.U. Amorpha-4,11-diene synthase of Artemisia annua: cDNA isolation and bacterial expression of a terpene synthase involved in artemisinin biosynthesis. Arch. Biochem. Biophys. 383 (2000) 178–184. [DOI] [PMID: 11185551]
5.  Martin, V.J., Pitera, D.J., Withers, S.T., Newman, J.D. and Keasling, J.D. Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nat. Biotechnol. 21 (2003) 796–802. [DOI] [PMID: 12778056]
6.  Picaud, S., Mercke, P., He, X., Sterner, O., Brodelius, M., Cane, D.E. and Brodelius, P.E. Amorpha-4,11-diene synthase: Mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate. Arch. Biochem. Biophys. 448 (2006) 150–155. [DOI] [PMID: 16143293]
[EC 4.2.3.24 created 2006]
 
 
EC 4.2.3.25     
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]
[EC 4.2.3.25 created 2006]
 
 
EC 4.2.3.26     
Accepted name: R-linalool synthase
Reaction: geranyl diphosphate + H2O = (3R)-linalool + diphosphate
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: (3R)-linalool = (3R)-3,7-dimethylocta-1,6-dien-3-ol
Other name(s): (3R)-linalool synthase; (–)-3R-linalool synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [(3R)-linalool-forming]
Comments: Geranyl diphosphate cannot be replaced by isopentenyl diphosphate (3-methylbut-3-en-1-yl diphosphate), prenyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrate [1]. Requires Mg2+ or Mn2+ for activity. Unlike many other monoterpene synthases, only a single product, (3R)-linalool, is formed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 254993-26-5
References:
1.  Jia, J.W., Crock, J., Lu, S., Croteau, R. and Chen, X.Y. (3R)-Linalool synthase from Artemisia annua L.: cDNA isolation, characterization, and wound induction. Arch. Biochem. Biophys. 372 (1999) 143–149. [DOI] [PMID: 10562427]
2.  Crowell, A.L., Williams, D.C., Davis, E.M., Wildung, M.R. and Croteau, R. Molecular cloning and characterization of a new linalool synthase. Arch. Biochem. Biophys. 405 (2002) 112–121. [DOI] [PMID: 12176064]
[EC 4.2.3.26 created 2006]
 
 
EC 4.2.3.36     
Accepted name: terpentetriene synthase
Reaction: terpentedienyl diphosphate = terpentetriene + diphosphate
For diagram of diterpenoid biosynthesis, click here
Other name(s): Cyc2 (ambiguous)
Systematic name: terpentedienyl-diphosphate diphosphate-lyase (terpentetriene-forming)
Comments: Requires Mg2+ for maximal activity but can use Mn2+, Fe2+ or Co2+ to a lesser extent [2]. Following on from EC 5.5.1.15, terpentedienyl-diphosphate synthase, this enzyme completes the transformation of geranylgeranyl diphosphate (GGDP) into terpentetriene, which is a precursor of the diterpenoid antibiotic terpentecin. Farnesyl diphosphate can also act as a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dairi, T., Hamano, Y., Kuzuyama, T., Itoh, N., Furihata, K. and Seto, H. Eubacterial diterpene cyclase genes essential for production of the isoprenoid antibiotic terpentecin. J. Bacteriol. 183 (2001) 6085–6094. [DOI] [PMID: 11567009]
2.  Hamano, Y., Kuzuyama, T., Itoh, N., Furihata, K., Seto, H. and Dairi, T. Functional analysis of eubacterial diterpene cyclases responsible for biosynthesis of a diterpene antibiotic, terpentecin. J. Biol. Chem. 277 (2002) 37098–37104. [DOI] [PMID: 12138123]
3.  Eguchi, T., Dekishima, Y., Hamano, Y., Dairi, T., Seto, H. and Kakinuma, K. A new approach for the investigation of isoprenoid biosynthesis featuring pathway switching, deuterium hyperlabeling, and 1H NMR spectroscopy. The reaction mechanism of a novel streptomyces diterpene cyclase. J. Org. Chem. 68 (2003) 5433–5438. [DOI] [PMID: 12839434]
[EC 4.2.3.36 created 2008]
 
 
EC 4.2.3.38     
Accepted name: α-bisabolene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (E)-α-bisabolene + diphosphate
For diagram of bisabolene-derived sesquiterpenoid biosynthesis, click here
Other name(s): bisabolene synthase
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(E)-α-bisabolene-forming]
Comments: This cytosolic sesquiterpenoid synthase requires a divalent cation cofactor (Mg2+ or, to a lesser extent, Mn2+) to neutralize the negative charge of the diphosphate leaving group. While unlikely to encounter geranyl diphosphate (GDP) in vivo as it is localized to plastids, the enzyme can use GDP as a substrate in vitro to produce (+)-(4R)-limonene [cf. EC 4.2.3.20, (R)-limonene synthase]. The enzyme is induced as part of a defense mechanism in the grand fir Abies grandis as a response to stem wounding.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bohlmann, J., Crock, J., Jetter, R. and Croteau, R. Terpenoid-based defenses in conifers: cDNA cloning, characterization, and functional expression of wound-inducible (E)-α-bisabolene synthase from grand fir (Abies grandis). Proc. Natl. Acad. Sci. USA 95 (1998) 6756–6761. [DOI] [PMID: 9618485]
[EC 4.2.3.38 created 2009]
 
 
EC 4.2.3.41     
Accepted name: elisabethatriene synthase
Reaction: geranylgeranyl diphosphate = elisabethatriene + diphosphate
For diagram of diterpenoid biosynthesis, click here and for reaction mechanism, click here
Other name(s): elisabethatriene cyclase
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (elisabethatriene-forming)
Comments: Requires Mg2+ or less efficiently Mn2+. The enzyme is also able to use farnesyl diphosphate and geranyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 334022-59-2
References:
1.  Kohl, A.C. and Kerr, R.G. Identification and characterization of the pseudopterosin diterpene cyclase, elisabethatriene synthase, from the marine gorgonian, Pseudopterogorgia elisabethae. Arch. Biochem. Biophys. 424 (2004) 97–104. [DOI] [PMID: 15019841]
2.  Bruck, T.B. and Kerr, R.G. Purification and kinetic properties of elisabethatriene synthase from the coral Pseudopterogorgia elisabethae. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 143 (2006) 269–278. [DOI] [PMID: 16423548]
[EC 4.2.3.41 created 2009]
 
 
EC 4.2.3.43     
Accepted name: fusicocca-2,10(14)-diene synthase
Reaction: geranylgeranyl diphosphate = fusicocca-2,10(14)-diene + diphosphate
For diagram of diterpenoid biosynthesis, click here and for reaction mechanism, click here
Other name(s): fusicoccadiene synthase; PaFS; PaDC4
Systematic name: geranylgeranyl diphosphate-lyase (fusicocca-2,10(14)-diene-forming)
Comments: A multifunctional enzyme with EC 2.5.1.29 farnesyltranstransferase activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Toyomasu, T., Tsukahara, M., Kaneko, A., Niida, R., Mitsuhashi, W., Dairi, T., Kato, N. and Sassa, T. Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi. Proc. Natl. Acad. Sci. USA 104 (2007) 3084–3088. [DOI] [PMID: 17360612]
[EC 4.2.3.43 created 2009]
 
 
EC 4.2.3.51     
Accepted name: β-phellandrene synthase (neryl-diphosphate-cyclizing)
Reaction: neryl diphosphate = β-phellandrene + diphosphate
Other name(s): phellandrene synthase 1; PHS1; monoterpene synthase PHS1
Systematic name: neryl-diphosphate diphosphate-lyase [cyclizing; β-phellandrene-forming]
Comments: The enzyme from Solanum lycopersicum has very poor affinity with geranyl diphosphate as substrate. Catalyses the formation of the acyclic myrcene and ocimene as major products in addition to β-phellandrene [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schilmiller, A.L., Schauvinhold, I., Larson, M., Xu, R., Charbonneau, A.L., Schmidt, A., Wilkerson, C., Last, R.L. and Pichersky, E. Monoterpenes in the glandular trichomes of tomato are synthesized from a neryl diphosphate precursor rather than geranyl diphosphate. Proc. Natl. Acad. Sci. USA 106 (2009) 10865–10870. [DOI] [PMID: 19487664]
[EC 4.2.3.51 created 2010]
 
 
EC 4.2.3.52     
Accepted name: (4S)-β-phellandrene synthase (geranyl-diphosphate-cyclizing)
Reaction: geranyl diphosphate = (4S)-β-phellandrene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Other name(s): phellandrene synthase; (-)-β-phellandrene synthase; (-)-(4S)-β-phellandrene synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing; (4S)-β-phellandrene-forming]
Comments: Requires Mn2+. Mg2+ is not effective [1]. Some (-)-α-phellandrene is also formed [3]. The reaction involves a 1,3-hydride shift [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 137010-34-5
References:
1.  Savage, T.J., Hatch, M.W. and Croteau, R. Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase. J. Biol. Chem. 269 (1994) 4012–4020. [PMID: 8307957]
2.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [DOI] [PMID: 10441373]
3.  Wagschal, K., Savage, T.J. and Croteau, R. Isotopically sensitive branching as a tool for evaluating multiple product formation by monoterpene cyclases. Tetrahedron 31 (1991) 5933–5944.
4.  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 4.2.3.52 created 2010]
 
 
EC 4.2.3.105     
Accepted name: tricyclene synthase
Reaction: geranyl diphosphate = tricyclene + diphosphate
For diagram of bornane and related monoterpenoids, click here
Other name(s): TPS3
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing; tricyclene-forming)
Comments: The enzyme from Solanum lycopersicum (tomato) gives a mixture of tricyclene, camphene, β-myrcene, limonene, and traces of several other monoterpenoids. See EC 4.2.3.117. (-)-camphene synthase, EC 4.2.3.15, myrcene synthase and EC 4.2.3.16, (4S)-limonene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Falara, V., Akhtar, T.A., Nguyen, T.T., Spyropoulou, E.A., Bleeker, P.M., Schauvinhold, I., Matsuba, Y., Bonini, M.E., Schilmiller, A.L., Last, R.L., Schuurink, R.C. and Pichersky, E. The tomato terpene synthase gene family. Plant Physiol. 157 (2011) 770–789. [DOI] [PMID: 21813655]
[EC 4.2.3.105 created 2012]
 
 
EC 4.2.3.106     
Accepted name: (E)-β-ocimene synthase
Reaction: geranyl diphosphate = (E)-β-ocimene + diphosphate
Glossary: (E)-β-ocimene = (3E)-3,7-dimethylocta-1,3,6-triene
Other name(s): β-ocimene synthase; AtTPS03; ama0a23; LjEβOS; MtEBOS
Systematic name: geranyl-diphosphate diphosphate-lyase [(E)-β-ocimene-forming]
Comments: Widely distributed in plants, which release β-ocimene when attacked by herbivorous insects.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Faldt, J., Arimura, G., Gershenzon, J., Takabayashi, J. and Bohlmann, J. Functional identification of AtTPS03 as (E)-β-ocimene synthase: a monoterpene synthase catalyzing jasmonate- and wound-induced volatile formation in Arabidopsis thaliana. Planta 216 (2003) 745–751. [DOI] [PMID: 12624761]
2.  Dudareva, N., Martin, D., Kish, C.M., Kolosova, N., Gorenstein, N., Faldt, J., Miller, B. and Bohlmann, J. (E)-β-ocimene and myrcene synthase genes of floral scent biosynthesis in snapdragon: function and expression of three terpene synthase genes of a new terpene synthase subfamily. Plant Cell 15 (2003) 1227–1241. [DOI] [PMID: 12724546]
3.  Arimura, G., Ozawa, R., Kugimiya, S., Takabayashi, J. and Bohlmann, J. Herbivore-induced defense response in a model legume. Two-spotted spider mites induce emission of (E)-β-ocimene and transcript accumulation of (E)-β-ocimene synthase in Lotus japonicus. Plant Physiol. 135 (2004) 1976–1983. [DOI] [PMID: 15310830]
4.  Navia-Gine, W.G., Yuan, J.S., Mauromoustakos, A., Murphy, J.B., Chen, F. and Korth, K.L. Medicago truncatula (E)-β-ocimene synthase is induced by insect herbivory with corresponding increases in emission of volatile ocimene. Plant Physiol. Biochem. 47 (2009) 416–425. [DOI] [PMID: 19249223]
[EC 4.2.3.106 created 2012]
 
 
EC 4.2.3.107     
Accepted name: (+)-car-3-ene synthase
Reaction: geranyl diphosphate = (+)-car-3-ene + diphosphate
For diagram of monoterpenoid biosynthesis, click here
Glossary: (+)-car-3-ene = (1S,6R)-3,7,7-trimethylbicyclo[4.1.0]hept-3-ene
Other name(s): 3-carene cyclase; 3-carene synthase; 3CAR; (+)-3-carene synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]
Comments: The enzyme reacts with (3S)-linalyl diphosphate twice as rapidly as geranyl diphosphate, but 25 times as rapidly as (3R)-linalyl diphosphate. It is assumed that (3S)-linalyl diphosphate is normally formed as an enzyme bound intermediate in the reaction. In the reaction the 5-pro-R hydrogen of geranyl diphosphate is eliminated during cyclopropane ring formation [1,2]. In Picea abies (Norway spruce) and Picea sitchensis (Sitka spruce) terpinolene is also formed [4,6]. See EC 4.2.3.113 terpinolene synthase. (+)-Car-3-ene is associated with resistance of Picea sitchensis (Sitka spruce) to white pine weevil [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Savage, T.J. and Croteau, R. Biosynthesis of monoterpenes: regio- and stereochemistry of (+)-3-carene biosynthesis. Arch. Biochem. Biophys. 305 (1993) 581–587. [DOI] [PMID: 8373196]
2.  Savage, T.J., Ichii, H., Hume, S.D., Little, D.B. and Croteau, R. Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents. Arch. Biochem. Biophys. 320 (1995) 257–265. [DOI] [PMID: 7625832]
3.  Savage, T.J., Hatch, M.W. and Croteau, R. Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase. J. Biol. Chem. 269 (1994) 4012–4020. [PMID: 8307957]
4.  Faldt, J., Martin, D., Miller, B., Rawat, S. and Bohlmann, J. Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase. Plant Mol. Biol. 51 (2003) 119–133. [PMID: 12602896]
5.  Hamberger, B., Hall, D., Yuen, M., Oddy, C., Hamberger, B., Keeling, C.I., Ritland, C., Ritland, K. and Bohlmann, J. Targeted isolation, sequence assembly and characterization of two white spruce (Picea glauca) BAC clones for terpenoid synthase and cytochrome P450 genes involved in conifer defence reveal insights into a conifer genome. BMC Plant Biol. 9:106 (2009). [DOI] [PMID: 19656416]
6.  Hall, D.E., Robert, J.A., Keeling, C.I., Domanski, D., Quesada, A.L., Jancsik, S., Kuzyk, M.A., Hamberger, B., Borchers, C.H. and Bohlmann, J. An integrated genomic, proteomic and biochemical analysis of (+)-3-carene biosynthesis in Sitka spruce (Picea sitchensis) genotypes that are resistant or susceptible to white pine weevil. Plant J. 65 (2011) 936–948. [DOI] [PMID: 21323772]
[EC 4.2.3.107 created 2012]
 
 
EC 4.2.3.108     
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]
[EC 4.2.3.108 created 2012]
 
 
EC 4.2.3.109     
Accepted name: (-)-sabinene synthase
Reaction: geranyl diphosphate = (-)-sabinene + diphosphate
For diagram of thujane monoterpenoid biosynthesis, click here
Glossary: (-)-sabinene = (1S,5S)-1-isopropyl-4-methylenebicyclo[3.1.0]hexane
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-sabinene-forming]
Comments: Requires Mg2+. Isolated from Pinus contorta (lodgepole pine) as cyclase I [1] and from Conocephalum conicum (liverwort) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Savage, T.J., Hatch, M.W. and Croteau, R. Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase. J. Biol. Chem. 269 (1994) 4012–4020. [PMID: 8307957]
2.  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]
[EC 4.2.3.109 created 2012]
 
 
EC 4.2.3.110     
Accepted name: (+)-sabinene synthase
Reaction: geranyl diphosphate = (+)-sabinene + diphosphate
For diagram of thujane monoterpenoid biosynthesis, click here
Glossary: (+)-sabinene = (+)-thuj-4(10)-ene = (1R,5R)-1-isopropyl-4-methylenebicyclo[3.1.0]hexane
Other name(s): SS
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-sabinene-forming]
Comments: Isolated from Salvia officinalis (sage). The recombinant enzyme gave 63% (+)-sabinene, 21% γ-terpinene, and traces of other monoterpenoids. See EC 4.2.3.114 γ-terpinene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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]
2.  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]
[EC 4.2.3.110 created 2012]
 
 
EC 4.2.3.111     
Accepted name: (-)-α-terpineol synthase
Reaction: geranyl diphosphate + H2O = (-)-α-terpineol + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-α-terpineol-forming]
Comments: The enzyme has been characterized from Vitis vinifera (grape). Also forms some 1,8-cineole and traces of other monoterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Martin, D.M. and Bohlmann, J. Identification of Vitis vinifera (-)-α-terpineol synthase by in silico screening of full-length cDNA ESTs and functional characterization of recombinant terpene synthase. Phytochemistry 65 (2004) 1223–1229. [DOI] [PMID: 15184006]
2.  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]
[EC 4.2.3.111 created 2012]
 
 
EC 4.2.3.112     
Accepted name: (+)-α-terpineol synthase
Reaction: geranyl diphosphate + H2O = (+)-α-terpineol + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-terpineol-forming]
Comments: The enzyme has been characterized from Santalum album (sandalwood). Also forms some (-)-limonene and traces of other monoterpenoids. See EC 4.2.3.16 (4S)-limonene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jones, C.G., Keeling, C.I., Ghisalberti, E.L., Barbour, E.L., Plummer, J.A. and Bohlmann, J. Isolation of cDNAs and functional characterisation of two multi-product terpene synthase enzymes from sandalwood, Santalum album L. Arch. Biochem. Biophys. 477 (2008) 121–130. [DOI] [PMID: 18541135]
[EC 4.2.3.112 created 2012]
 
 
EC 4.2.3.113     
Accepted name: terpinolene synthase
Reaction: geranyl diphosphate = terpinolene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: terpinolene = 1-methyl-4-(propan-2-ylidene)cyclohexene
Other name(s): ag9; PmeTPS2; LaLIMS_RR
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, terpinolene-forming)
Comments: Requires Mg2+. Mn2+ is less effective and product ratio changes. Forms traces of other monoterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
2.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [DOI] [PMID: 10441373]
3.  Faldt, J., Martin, D., Miller, B., Rawat, S. and Bohlmann, J. Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase. Plant Mol. Biol. 51 (2003) 119–133. [PMID: 12602896]
4.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [DOI] [PMID: 15921711]
5.  Landmann, C., Fink, B., Festner, M., Dregus, M., Engel, K.H. and Schwab, W. Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia). Arch. Biochem. Biophys. 465 (2007) 417–429. [DOI] [PMID: 17662687]
[EC 4.2.3.113 created 2012]
 
 
EC 4.2.3.114     
Accepted name: γ-terpinene synthase
Reaction: geranyl diphosphate = γ-terpinene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: γ-terpinene = 1-isopropyl-4-methylcyclohexa-1,4-diene
Other name(s): OvTPS2; ClcTS
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, γ-terpinene-forming)
Comments: Isolated from Thymus vulgaris (thyme) [1,2], Citrus limon (lemon) [3], Citrus unshiu (satsuma) [4] and Origanum vulgare (oregano) [5]. Requires Mg2+. Mn2+ less effective. The reaction involves a 1,2-hydride shift. The 5-pro-S hydrogen of geranyl diphosphate is lost. Traces of several other monoterpenoids are formed in addition to γ-terpinene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Alonso, W.R. and Croteau, R. Purification and characterization of the monoterpene cyclase γ-terpinene synthase from Thymus vulgaris. Arch. Biochem. Biophys. 286 (1991) 511–517. [DOI] [PMID: 1897973]
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]
3.  Lücker, J., El Tamer, M.K., Schwab, W., Verstappen, F.W., van der Plas, L.H., Bouwmeester, H.J. and Verhoeven, H.A. Monoterpene biosynthesis in lemon (Citrus limon). cDNA isolation and functional analysis of four monoterpene synthases. Eur. J. Biochem. 269 (2000) 3160–3171. [DOI] [PMID: 12084056]
4.  Suzuki, Y., Sakai, H., Shimada, T., Omura, M., Kumazawa, S. and Nakayama, T. Characterization of γ-terpinene synthase from Citrus unshiu (Satsuma mandarin). Biofactors 21 (2004) 79–82. [PMID: 15630174]
5.  Crocoll, C., Asbach, J., Novak, J., Gershenzon, J. and Degenhardt, J. Terpene synthases of oregano (Origanum vulgare L.) and their roles in the pathway and regulation of terpene biosynthesis. Plant Mol. Biol. 73 (2010) 587–603. [DOI] [PMID: 20419468]
[EC 4.2.3.114 created 2012]
 
 
EC 4.2.3.115     
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]
 
 
EC 4.2.3.116     
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 4.2.3.117     
Accepted name: (-)-camphene synthase
Reaction: geranyl diphosphate = (-)-camphene + diphosphate
Glossary: (-)-camphene = (1S,4R)-2,2-dimethyl-3-methylenebicyclo[2.2.1]heptane
Other name(s): CS
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-camphene-forming]
Comments: (-)-Camphene is the major product in Abies grandis (grand fir) with traces of other monoterpenoids [1]. In Pseudotsuga menziesii (Douglas-fir) there are about equal parts of (-)-camphene and (-)-α-pinene with traces of four other monoterpenoids [2,3]. In Solanum lycopersicum (tomato) tricyclene, β-myrcene, limonene, and traces of several other monoterpenoids are also formed [4]. See also EC 4.2.3.15 myrcene synthase, EC 4.2.3.16 (4S)-limonene synthase, EC 4.2.3.119 (-)-α-pinene synthase and EC 4.2.3.105 tricyclene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [DOI] [PMID: 10441373]
2.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [DOI] [PMID: 15921711]
3.  Hyatt, D.C. and Croteau, R. Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis. Arch. Biochem. Biophys. 439 (2005) 222–233. [DOI] [PMID: 15978541]
4.  Falara, V., Akhtar, T.A., Nguyen, T.T., Spyropoulou, E.A., Bleeker, P.M., Schauvinhold, I., Matsuba, Y., Bonini, M.E., Schilmiller, A.L., Last, R.L., Schuurink, R.C. and Pichersky, E. The tomato terpene synthase gene family. Plant Physiol. 157 (2011) 770–789. [DOI] [PMID: 21813655]
[EC 4.2.3.117 created 2012]
 
 
EC 4.2.3.118     
Accepted name: 2-methylisoborneol synthase
Reaction: (E)-2-methylgeranyl diphosphate + H2O = 2-methylisoborneol + diphosphate
For diagram of bornane and related monoterpenoids, click here and for diagram of reaction, click here
Other name(s): sco7700; 2-MIB cyclase; MIB synthase; MIBS
Systematic name: (E)-2-methylgeranyl-diphosphate diphosphate-lyase (cyclizing, 2-methylisoborneol-forming)
Comments: The product, 2-methylisoborneol, is a characteristc odiferous compound with a musty smell produced by soil microorganisms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Wang, C.M. and Cane, D.E. Biochemistry and molecular genetics of the biosynthesis of the earthy odorant methylisoborneol in Streptomyces coelicolor. J. Am. Chem. Soc. 130 (2008) 8908–8909. [DOI] [PMID: 18563898]
2.  Komatsu, M., Tsuda, M., Omura, S., Oikawa, H. and Ikeda, H. Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol. Proc. Natl. Acad. Sci. USA 105 (2008) 7422–7427. [DOI] [PMID: 18492804]
3.  Giglio, S., Chou, W.K., Ikeda, H., Cane, D.E. and Monis, P.T. Biosynthesis of 2-methylisoborneol in cyanobacteria. Environ. Sci. Technol. 45 (2011) 992–998. [DOI] [PMID: 21174459]
[EC 4.2.3.118 created 2012]
 
 
EC 4.2.3.119     
Accepted name: (-)-α-pinene synthase
Reaction: geranyl diphosphate = (-)-α-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (-)-α-pinene = (1S,5S)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene
Other name(s): (-)-α-pinene/(-)-camphene synthase; (-)-α-pinene cyclase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-α-pinene-forming]
Comments: Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-α-pinene, (-)-β-pinene and (-)-camphene, plus traces of other monoterpenoids. (3S)-Linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate. The 4-pro-S-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-6]. The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-α-pinene and (-)-β-pinene. However the clone ag11 gave 35% (-)-limonene, 24% (-)-α-pinene and 20% (-)-β-phellandrene. It requires Mn2+ and K+ (Mg2+ is ineffective) [7-10]. Synthase I from Pinus taeda (loblolly pine) produces (-)-α-pinene with traces of (-)-β-pinene and requires Mn2+ (preferred to Mg2+) [11,12]. The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-α-pinene and 30% (-)-β-pinene [13]. The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-α-pinene and (-)-camphene plus traces of other monoterpenoids [14]. See also EC 4.2.3.120, (-)-β-pinene synthase; EC 4.2.3.117, (-)-camphene synthase; EC 4.2.3.16, (-)-limonene synthase; and EC 4.2.3.52, (-)-β-phellandrene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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.B., Wheeler, C.J., Cane, D.E., Ebert, R. and Ha, H.J. Isotopically sensitive branching in the formation of cyclic monoterpenes: proof that (-)-α-pinene and (-)-β-pinene are synthesized by the same monoterpene cyclase via deprotonation of a common intermediate. Biochemistry 26 (1987) 5383–5389. [PMID: 3314988]
3.  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]
4.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
5.  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]
6.  Lu, S., Xu, R., Jia, J.W., Pang, J., Matsuda, S.P. and Chen, X.Y. Cloning and functional characterization of a β-pinene synthase from Artemisia annua that shows a circadian pattern of expression. Plant Physiol. 130 (2002) 477–486. [DOI] [PMID: 12226526]
7.  Lewinsohn, E., Gijzen, M. and Croteau, R. Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE. Arch. Biochem. Biophys. 293 (1992) 167–173. [DOI] [PMID: 1731633]
8.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [DOI] [PMID: 9268308]
9.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [DOI] [PMID: 10441373]
10.  Hyatt, D.C. and Croteau, R. Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis. Arch. Biochem. Biophys. 439 (2005) 222–233. [DOI] [PMID: 15978541]
11.  Phillips, M.A., Savage, T.J. and Croteau, R. Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers. Arch. Biochem. Biophys. 372 (1999) 197–204. [DOI] [PMID: 10562434]
12.  Phillips, M.A., Wildung, M.R., Williams, D.C., Hyatt, D.C. and Croteau, R. cDNA isolation, functional expression, and characterization of (+)-α-pinene synthase and (-)-α-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis. Arch. Biochem. Biophys. 411 (2003) 267–276. [DOI] [PMID: 12623076]
13.  McKay, S.A., Hunter, W.L., Godard, K.A., Wang, S.X., Martin, D.M., Bohlmann, J. and Plant, A.L. Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce. Plant Physiol. 133 (2003) 368–378. [DOI] [PMID: 12970502]
14.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [DOI] [PMID: 15921711]
[EC 4.2.3.119 created 2012]
 
 
EC 4.2.3.120     
Accepted name: (-)-β-pinene synthase
Reaction: geranyl diphosphate = (-)-β-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (-)-β-pinene = (1S,5S)-6,6-dimethyl-2-methylenebicyclo[3.1.1]hept-2-ene
Other name(s): β-geraniolene synthase; (-)-(1S,5S)-pinene synthase; geranyldiphosphate diphosphate lyase (pinene forming)
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-β-pinene-forming]
Comments: Cyclase II of Salvia officinalis (sage) produces about equal parts (-)-α-pinene, (-)-β-pinene and (-)-camphene, plus traces of other monoterpenoids. The enzyme, which requires Mg2+ (preferred to Mn2+), can also use (3S)-Linalyl diphosphate (preferred to (3R)-linalyl diphosphate) [1-4]. The enzyme from Abies grandis (grand fir) produces roughly equal parts of (-)-α-pinene and (-)-β-pinene [6-9]. Cyclase IV from Pinus contorta (lodgepole pine) produces 63% (-)-β-pinene, 26% 3-carene, and traces of α-pinene [10]. Synthase III from Pinus taeda (loblolly pine) forms (-)-β-pinene with traces of α-pinene and requires Mn2+ and K+ (Mg2+ is ineffective) [11]. A cloned enzyme from Artemisia annua (sweet wormwood) gave (-)-β-pinene with traces of (-)-α-pinene [5]. The enzyme from Picea sitchensis (Sika spruce) forms 30% (-)-β-pinene and 70% (-)-α-pinene [12]. See also EC 4.2.3.119, (-)-α-pinene synthase, EC 4.2.3.117, (-)-camphene synthase, and EC 4.2.3.107 (+)-3-carene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Croteau, R.B., Wheeler, C.J., Cane, D.E., Ebert, R. and Ha, H.J. Isotopically sensitive branching in the formation of cyclic monoterpenes: proof that (-)-α-pinene and (-)-β-pinene are synthesized by the same monoterpene cyclase via deprotonation of a common intermediate. Biochemistry 26 (1987) 5383–5389. [PMID: 3314988]
2.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
3.  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]
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]
5.  Lu, S., Xu, R., Jia, J.W., Pang, J., Matsuda, S.P. and Chen, X.Y. Cloning and functional characterization of a β-pinene synthase from Artemisia annua that shows a circadian pattern of expression. Plant Physiol. 130 (2002) 477–486. [DOI] [PMID: 12226526]
6.  Gijzen, M., Lewinsohn, E. and Croteau, R. Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis). Arch. Biochem. Biophys. 289 (1991) 267–273. [DOI] [PMID: 1898071]
7.  Lewinsohn, E., Gijzen, M. and Croteau, R. Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE. Arch. Biochem. Biophys. 293 (1992) 167–173. [DOI] [PMID: 1731633]
8.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [DOI] [PMID: 9268308]
9.  Hyatt, D.C. and Croteau, R. Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis. Arch. Biochem. Biophys. 439 (2005) 222–233. [DOI] [PMID: 15978541]
10.  Savage, T.J., Ichii, H., Hume, S.D., Little, D.B. and Croteau, R. Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents. Arch. Biochem. Biophys. 320 (1995) 257–265. [DOI] [PMID: 7625832]
11.  Phillips, M.A., Savage, T.J. and Croteau, R. Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers. Arch. Biochem. Biophys. 372 (1999) 197–204. [DOI] [PMID: 10562434]
12.  McKay, S.A., Hunter, W.L., Godard, K.A., Wang, S.X., Martin, D.M., Bohlmann, J. and Plant, A.L. Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce. Plant Physiol. 133 (2003) 368–378. [DOI] [PMID: 12970502]
[EC 4.2.3.120 created 2012]
 
 
EC 4.2.3.121     
Accepted name: (+)-α-pinene synthase
Reaction: geranyl diphosphate = (+)-α-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (+)-α-pinene = (1R,5R)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene
Other name(s): (+)-α-pinene cyclase; cyclase I
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-pinene-forming]
Comments: Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-α-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-α-pinene and (+)-β-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. The 4-pro-R-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-4]. With synthase II of Pinus taeda (loblolly pine) (+)-α-pinene was the only product [5,6]. Requires Mn2+ (preferred to Mg2+). See also EC 4.2.3.122, (+)-β-pinene synthase, and EC 4.2.3.116, (+)-camphene 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]
5.  Phillips, M.A., Savage, T.J. and Croteau, R. Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers. Arch. Biochem. Biophys. 372 (1999) 197–204. [DOI] [PMID: 10562434]
6.  Phillips, M.A., Wildung, M.R., Williams, D.C., Hyatt, D.C. and Croteau, R. cDNA isolation, functional expression, and characterization of (+)-α-pinene synthase and (-)-α-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis. Arch. Biochem. Biophys. 411 (2003) 267–276. [DOI] [PMID: 12623076]
[EC 4.2.3.121 created 2012]
 
 
EC 4.2.3.122     
Accepted name: (+)-β-pinene synthase
Reaction: geranyl diphosphate = (+)-β-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (+)-β-pinene = (1R,5R)-6,6-dimethyl-2-methylenebicyclo[3.1.1]hept-2-ene
Other name(s): (+)-pinene cyclase; cyclase III
Systematic name: geranyl-diphosphate diphosphate-lyase [(+)-β-pinene-forming]
Comments: Cyclase III from Salvia officinalis (sage) gives roughly equal parts of (+)-β-pinene and (+)-α-pinene. See EC 4.2.3.121, (+)-α-pinene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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]
2.  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 4.2.3.122 created 2012]
 
 
EC 4.2.3.141     
Accepted name: sclareol synthase
Reaction: (13E)-8α-hydroxylabd-13-en-15-yl diphosphate + H2O = sclareol + diphosphate
For diagram of hydroxylabdenyl diphosphate derived diterpenoids, click here
Glossary: sclareol = (13R)-labd-14-ene-8α,13-diol
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = 8-hydroxycopalyl diphosphate
Other name(s): SS
Systematic name: (13E)-8α-hydroxylabd-13-en-15-yl-diphosphate-lyase (sclareol-forming)
Comments: Isolated from the plant Salvia sclarea (clary sage). Originally thought to be synthesized in one step from geranylgeranyl diphosphate it is now known to require two enzymes, EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141, sclareol synthase. Sclareol is used in perfumery.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Caniard, A., Zerbe, P., Legrand, S., Cohade, A., Valot, N., Magnard, J.L., Bohlmann, J. and Legendre, L. Discovery and functional characterization of two diterpene synthases for sclareol biosynthesis in Salvia sclarea (L.) and their relevance for perfume manufacture. BMC Plant Biol. 12:119 (2012). [DOI] [PMID: 22834731]
[EC 4.2.3.141 created 2013, modified 2017]
 
 
EC 4.2.3.144     
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 4.2.3.146     
Accepted name: cyclooctat-9-en-7-ol synthase
Reaction: geranylgeranyl diphosphate + H2O = cyclooctat-9-en-7-ol + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: cyclooctat-9-en-7-ol = (1R,3aR,4S,7R,9aR,10aR)-1,4,9a-trimethyl-7-(propan-2-yl)-1,2,3,3a,4,5,7,8,9,9a,10,10a-dodecahydrodicyclopenta[a,d][8]annulen-4-ol
Other name(s): cotB2
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cyclooctat-9-en-7-ol-forming)
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces melanosporofaciens, where it is part of the biosynthesis of cyclooctatin, a potent inhibitor of lysophospholipase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kim, S.Y., Zhao, P., Igarashi, M., Sawa, R., Tomita, T., Nishiyama, M. and Kuzuyama, T. Cloning and heterologous expression of the cyclooctatin biosynthetic gene cluster afford a diterpene cyclase and two P450 hydroxylases. Chem. Biol. 16 (2009) 736–743. [DOI] [PMID: 19635410]
2.  Zhang, X., Shang, G., Gu, L. and Shen, Y. Crystallization and preliminary X-ray diffraction analysis of the diterpene cyclooctatin synthase (CYC) from Streptomyces sp. LZ35. Acta Crystallogr. F Struct. Biol. Commun. 70 (2014) 366–369. [DOI] [PMID: 24598929]
3.  Janke, R., Gorner, C., Hirte, M., Bruck, T. and Loll, B. The first structure of a bacterial diterpene cyclase: CotB2. Acta Crystallogr. D Biol. Crystallogr. 70 (2014) 1528–1537. [DOI] [PMID: 24914964]
4.  Meguro, A., Motoyoshi, Y., Teramoto, K., Ueda, S., Totsuka, Y., Ando, Y., Tomita, T., Kim, S.Y., Kimura, T., Igarashi, M., Sawa, R., Shinada, T., Nishiyama, M. and Kuzuyama, T. An unusual terpene cyclization mechanism involving a carbon-carbon bond rearrangement. Angew. Chem. Int. Ed. Engl. 54 (2015) 4353–4356. [DOI] [PMID: 25689152]
5.  Tomita, T., Kim, S.Y., Teramoto, K., Meguro, A., Ozaki, T., Yoshida, A., Motoyoshi, Y., Mori, N., Ishigami, K., Watanabe, H., Nishiyama, M. and Kuzuyama, T. Structural Insights into the CotB2-catalyzed cyclization of geranylgeranyl diphosphate to the diterpene cyclooctat-9-en-7-ol. ACS Chem. Biol. 12 (2017) 1621–1628. [DOI] [PMID: 28463490]
[EC 4.2.3.146 created 2014]
 
 
EC 4.2.3.148     
Accepted name: cembrene C synthase
Reaction: geranylgeranyl diphosphate = cembrene C + diphosphate
For diagram of cembrene and related diterpenoids, click here
Glossary: cembrene C = (1E,5E,9E)-1,5,9-trimethyl-12-(propan-2-ylidene)cyclotetradeca-1,5,9-triene
Other name(s): DtcycA (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cembrene-C-forming)
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This bifunctional enzyme also produces (R)-nephthenol. See EC 4.2.3.149, nephthenol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. ChemBioChem 14 (2013) 316–321. [DOI] [PMID: 23386483]
[EC 4.2.3.148 created 2014]
 
 
EC 4.2.3.149     
Accepted name: nephthenol synthase
Reaction: geranylgeranyl diphosphate + H2O = (R)-nephthenol + diphosphate
For diagram of cembrene and related diterpenoids, click here
Glossary: (R)-nephthenol = 2-[(1R,3E,7E,11E)-4,8,12-trimethyltetradeca-3,7,11-trien-1-yl]propan-2-ol
Other name(s): DtcycA (gene name); DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(R)-nephthenol-forming]
Comments: Requires Mg2+. Two isozymes with this activity were isolated from the bacterium Streptomyces sp. SANK 60404. The enzyme encoded by the DtcycA gene also produces cembrene C (see EC 4.2.3.148, cembrene C synthase), while the enzyme encoded by the DtcycB gene also produces (R)-cembrene A and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol (see EC 4.2.3.150, cembrene A synthase, and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. ChemBioChem 14 (2013) 316–321. [DOI] [PMID: 23386483]
[EC 4.2.3.149 created 2014]
 
 
EC 4.2.3.150     
Accepted name: cembrene A synthase
Reaction: geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
For diagram of cembrene and related diterpenoids, click here
Glossary: cembrene A = (1E,5E,9E,12R)-1,5,9-trimethyl-12-(propan-2-en-2-yl)cyclotetradeca-1,5,9-triene
Other name(s): DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(R)-cembrene-A-forming]
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. ChemBioChem 14 (2013) 316–321. [DOI] [PMID: 23386483]
[EC 4.2.3.150 created 2014]
 
 
EC 4.2.3.151     
Accepted name: pentamethylcyclopentadecatrienol synthase
Reaction: geranylgeranyl diphosphate + H2O = (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol + diphosphate
For diagram of cembrene and related diterpenoids, click here
Other name(s): DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol-forming]
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (R)-cembrene A. See EC 4.2.3.150, cembrene A synthase and EC 4.2.3.149, nephthenol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. ChemBioChem 14 (2013) 316–321. [DOI] [PMID: 23386483]
[EC 4.2.3.151 created 2014]
 
 
EC 4.2.3.158     
Accepted name: (–)-spiroviolene synthase
Reaction: geranylgeranyl diphosphate = (–)-spiroviolene + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: (–)-spiroviolene = (2R,3a′S,3b′R,5S,6a′R)-2,4′,4′,5,6a′-pentamethyl-2′,3′,3a′,3b′,4′,5′,6′,6a′-octahydrospiro[cyclopentane-1,1′-cyclopenta[a]pentalene]
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [cyclizing, (–)-spiroviolene-forming]
Comments: The enzyme, which forms the diterpene (–)-spiroviolene, has been characterized from the bacterium Streptomyces violens.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rabe, P., Rinkel, J., Dolja, E., Schmitz, T., Nubbemeyer, B., Luu, T.H. and Dickschat, J.S. Mechanistic investigations of two bacterial diterpene cyclases: spiroviolene synthase and tsukubadiene synthase. Angew. Chem. Int. Ed. Engl. 56 (2017) 2776–2779. [DOI] [PMID: 28146322]
2.  Xu, H. and Dickschat, J.S. Revision of the cyclisation mechanism for the diterpene spiroviolene and investigations of Its mass spectrometric fragmentation. Chembiochem 22 (2021) 850–854. [DOI] [PMID: 33084237]
[EC 4.2.3.158 created 2017]
 
 
EC 4.2.3.159     
Accepted name: tsukubadiene synthase
Reaction: geranylgeranyl diphosphate = tsukubadiene + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: tsukubadiene = (1S,3aS,5Z,7aS,10aR,11Z)-1,5,8,8,10a-pentamethyl-2,3,3a,4,7,7a,8,9,10,10a-decahydro-1H-dicyclopenta[a,d][9]annulene
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, tsukubadiene-forming)
Comments: The synthesis of the diterpene tsukubadiene has been shown to occur in the Actinobacterium Streptomyces tsukubaensis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamada, Y., Arima, S., Nagamitsu, T., Johmoto, K., Uekusa, H., Eguchi, T., Shin-ya, K., Cane, D.E. and Ikeda, H. Novel terpenes generated by heterologous expression of bacterial terpene synthase genes in an engineered Streptomyces host. J. Antibiot. (Tokyo) 68 (2015) 385–394. [DOI] [PMID: 25605043]
2.  Rabe, P., Rinkel, J., Dolja, E., Schmitz, T., Nubbemeyer, B., Luu, T.H. and Dickschat, J.S. Mechanistic investigations of two bacterial diterpene cyclases: spiroviolene synthase and tsukubadiene synthase. Angew. Chem. Int. Ed. Engl. 56 (2017) 2776–2779. [DOI] [PMID: 28146322]
[EC 4.2.3.159 created 2017]
 
 
EC 4.2.3.167     
Accepted name: dolabella-3,7-dien-18-ol synthase
Reaction: geranylgeranyl diphosphate + H2O = (3E,7E)-dolabella-3,7-dien-18-ol + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: (3E,7E)-dolabella-3,7-dien-18-ol = 2-[(1R,3aR,5E,9E,12aR)-3a,6,10-trimethyl-1,2,3,3a,4,7,8,11,12,12a-decahydrocyclopenta[11]annulen-1-yl]propan-2-ol
Other name(s): TPS20 (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [cyclizing, (3E,7E)-dolabella-3,7-dien-18-ol-forming]
Comments: Isolated from an ecotype of the plant Arabidopsis thaliana from Cape Verde Islands. The enzyme also gives (3E,7E)-dolathalia-3,7,11-triene and traces of other terpenoids. cf. EC 4.2.3.168 dolathalia-3,7,11-triene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Q., Jia, M., Huh, J.H., Muchlinski, A., Peters, R.J. and Tholl, D. Identification of a dolabellane type diterpene synthase and other root-expressed diterpene synthases in Arabidopsis. Front. Plant Sci. 7:1761 (2016). [DOI] [PMID: 27933080]
[EC 4.2.3.167 created 2017]
 
 
EC 4.2.3.168     
Accepted name: dolathalia-3,7,11-triene synthase
Reaction: geranylgeranyl diphosphate = (3E,7E)-dolathalia-3,7,11-triene + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: (3E,7E)-dolathalia-3,7,11-triene = (7E,11E)-3,3,7,11,13a-pentamethy1-2,3,5,6,9,10,13,13a-octahydro-1H-benzo[11]annulene
Other name(s): TPS20 (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [cyclizing, (3E,7E)-dolathalia-3,7,11-triene-forming]
Comments: Isolated from an ecotype of the plant Arabidopsis thaliana from Cape Verde Islands. The enzyme also gives (3E,7E)-dolabella-3,7-dien-18-ol and traces of other terpenoids. cf. EC 4.2.3.167 dolabella-3,7-dien-18-ol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Q., Jia, M., Huh, J.H., Muchlinski, A., Peters, R.J. and Tholl, D. Identification of a dolabellane type diterpene synthase and other root-expressed diterpene synthases in Arabidopsis. Front. Plant Sci. 7:1761 (2016). [DOI] [PMID: 27933080]
[EC 4.2.3.168 created 2017]
 
 
EC 4.2.3.177     
Accepted name: β-thujene synthase
Reaction: geranyl diphosphate = β-thujene + diphosphate
For diagram of thujane monoterpenoid biosynthesis, click here
Other name(s): CoTPS1
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, β-thujene-forming)
Comments: Isolated from the plant Cananga odorata var. fruticosa (ylang ylang). The enzyme forms roughly equal proportions of β-thujene, sabinene, β-pinene and α-terpinene see EC 4.2.3.109/EC 4.2.3.110 sabinene synthase, EC 4.2.3.120/EC 4.2.3.122 β-pinene synthase, EC 4.2.3.115 α-terpinene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jin, J., Kim, M.J., Dhandapani, S., Tjhang, J.G., Yin, J.L., Wong, L., Sarojam, R., Chua, N.H. and Jang, I.C. The floral transcriptome of ylang ylang (Cananga odorata var. fruticosa) uncovers biosynthetic pathways for volatile organic compounds and a multifunctional and novel sesquiterpene synthase. J. Exp. Bot. 66 (2015) 3959–3975. [DOI] [PMID: 25956881]
[EC 4.2.3.177 created 2017]
 
 
EC 4.2.3.180     
Accepted name: pseudolaratriene synthase
Reaction: geranylgeranyl diphosphate = pseudolaratriene + diphosphate
For diagram of miscellaneous diterpenoid biosynthesis, click here
Glossary: pseudolaradiene = (1RS,3aSR,8aRS)-3a,6-dimethyl-1-(6-methylhepta-2,5-dien-2-yl)-1,2,3,3a,4,7,8,8a-octahydrohydroazulene
Other name(s): PxaTPS8
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, pseudolaradiene-forming)
Comments: Isolated from the plant Pseudolarix amabilis (golden larch). The product is oxidized to pseudolaric acid B, a microtubule-destabilizing agent.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mafu, S., Karunanithi, P.S., Palazzo, T.A., Harrod, B.L., Rodriguez, S.M., Mollhoff, I.N., O'Brien, T.E., Tong, S., Fiehn, O., Tantillo, D.J., Bohlmann, J. and Zerbe, P. Biosynthesis of the microtubule-destabilizing diterpene pseudolaric acid B from golden larch involves an unusual diterpene synthase. Proc. Natl. Acad. Sci. USA 114 (2017) 974–979. [DOI] [PMID: 28096378]
[EC 4.2.3.180 created 2017]
 
 
EC 4.2.3.191     
Accepted name: cycloaraneosene synthase
Reaction: geranylgeranyl diphosphate = cycloaraneosene + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: cycloaraneosene = (1R,3aR,9aS,10aR)-1,9a-dimethyl-4-methylene-7-(propan-2-yl)-1,2,3,3a,4,5,6,8,9,9a,10,10a-dodecahydrodicyclopenta[a,d][8]annulene
Other name(s): SdnA
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cycloaraneosene-forming)
Comments: Isolated from the fungus Sordaria araneosa. Cycloaraneosene is a precursor of the antibiotic sordarin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kudo, F., Matsuura, Y., Hayashi, T., Fukushima, M. and Eguchi, T. Genome mining of the sordarin biosynthetic gene cluster from Sordaria araneosa Cain ATCC 36386: characterization of cycloaraneosene synthase and GDP-6-deoxyaltrose transferase. J. Antibiot. (Tokyo) 69 (2016) 541–548. [DOI] [PMID: 27072286]
[EC 4.2.3.191 created 2017]
 
 
EC 4.2.3.195     
Accepted name: rhizathalene A synthase
Reaction: geranylgeranyl diphosphate = rhizathalene A + diphosphate
For diagram of miscellaneous diterpenoid biosynthesis, click here
Other name(s): TPS08 (gene name)
Systematic name: geranygeranyl-diphosphate diphosphate-lyase (rhizathalene A-forming)
Comments: The enzyme was identified in the roots of the plant Arabidopsis thaliana (thale cress). The product is a semivolatile diterpene that acts as a local antifeedant in belowground direct defense against root-feeding insects.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vaughan, M.M., Wang, Q., Webster, F.X., Kiemle, D., Hong, Y.J., Tantillo, D.J., Coates, R.M., Wray, A.T., Askew, W., O'Donnell, C., Tokuhisa, J.G. and Tholl, D. Formation of the unusual semivolatile diterpene rhizathalene by the Arabidopsis class I terpene synthase TPS08 in the root stele is involved in defense against belowground herbivory. Plant Cell 25 (2013) 1108–1125. [DOI] [PMID: 23512856]
[EC 4.2.3.195 created 2017]
 
 


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