EC 4.2.3.51 to EC 4.2.3.100, EC 4.2.3.101 to EC 4.2.3.150 and EC 4.2.3.151 to EC 4.2.3.229.
Accepted name: threonine synthase
Reaction: O-phospho-L-homoserine + H2O = L-threonine + phosphate
For diagram click here.
Other name(s): threonine synthetase; O-phospho-L-homoserine phospho-lyase (adding water)
Systematic name: O-phospho-L-homoserine phosphate-lyase (adding water; L-threonine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-97-6
References:
1. Flavin, M. and Slaughter, C. Purification and properties of threonine synthetase of Neurospora. J. Biol. Chem. 235 (1960) 1103-1108. [PMID: 13823379]
Accepted name: ethanolamine-phosphate phospho-lyase
Reaction: ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate
Other name(s): O-phosphoethanolamine-phospholyase; amino alcohol O-phosphate phospholyase; O-phosphorylethanol-amine phospho-lyase; ethanolamine-phosphate phospho-lyase (deaminating)
Systematic name: ethanolamine-phosphate phosphate-lyase (deaminating; acetaldehyde-forming)
Comments: A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-88-3
References:
1. Fleshood, H.L. and Pitot, H.C. The metabolism of O-phosphorylethanolamine in animal tissues. I. O-Phosphorylethanolamine phospho-lyase: partial purification and characterization. J. Biol. Chem. 245 (1970) 4414-4420. [PMID: 5498429]
2. Jones, A., Faulkner, A. and Turner, J.M. Microbial metabolism of amino alcohols. Metabolism of ethanolamine and 1-aminopropan-2-ol in species of Erwinia and the roles of amino alcohol kinase and amino alcohol o-phosphate phospho-lyase in aldehyde formation. Biochem. J. 134 (1973) 959-968. [PMID: 4357716]
Accepted name: methylglyoxal synthase
Reaction: glycerone phosphate = methylglyoxal + phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
methylglyoxal = 2-oxopropanal
Other name(s): methylglyoxal synthetase; glycerone-phosphate phospho-lyase
Systematic name: glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Comments: Does not act on D-glyceraldehyde 3-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37279-01-9
References:
1. Cooper, R.A. and Anderson, A. The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli. FEBS Lett. 11 (1970) 273-276. [PMID: 11945504]
2. Hopper, D.J. and Cooper, R.A. The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis? FEBS Lett. 13 (1971) 213-216. [PMID: 11945670]
3. Ray, S. and Ray, M. Isolation of methylglyoxal synthase from goat liver. J. Biol. Chem. 256 (1981) 6230-6233. [PMID: 7240200]
Accepted name: 3-dehydroquinate synthase
Reaction: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
For diagram click here and mechanism here.
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): 5-dehydroquinate synthase; 5-dehydroquinic acid synthetase; dehydroquinate synthase; 3-dehydroquinate synthetase; 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing); 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Systematic name: 3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Comments: Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37211-77-1
References:
1. Rotenberg, S.L. and Sprinson, D.B. Mechanism and stereochemistry of 5-dehydroquinate synthetase. Proc. Natl. Acad. Sci. USA 67 (1970) 1669-1672. [PMID: 5275368]
2. Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate. J. Biol. Chem. 238 (1963) 3176-3182.
3. Bender, S.L., Mehdi, S. and Knowles, J.R. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28 (1989) 7555-7560. [PMID: 2514789]
4. Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 394 (1998) 299-302. [PMID: 9685163]
Accepted name: chorismate synthase
Reaction: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
For diagram click here and mechanism here.
Other name(s): 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase
Systematic name: 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase (chorismate-forming)
Comments: Requires FMN. The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH•). Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9077-07-0
References:
1. Gaertner, F.H. and Cole, K.W. Properties of chorismate synthase in Neurospora crassa. J. Biol. Chem. 248 (1973) 4602-4609. [PMID: 4146266]
2. Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate. J. Biol. Chem. 242 (1967) 82-90. [PMID: 4289188]
3. Welch, G.R., Cole, K.W. and Gaertner, F.H. Chorismate synthase of Neurospora crassa: a flavoprotein. Arch. Biochem. Biophys. 165 (1974) 505-518. [PMID: 4155270]
4. Bornemann, S., Lowe, D.J. and Thorneley, R.N. The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate. Biochemistry 35 (1996) 9907-9916. [PMID: 8703965]
5. Bornemann, S., Theoclitou, M.E., Brune, M., Webb, M.R., Thorneley, R.N. and Abell, C. A secondary β deuterium kinetic isotope effect in the chorismate synthase reaction. Bioorg. Chem. 28 (2000) 191-204. [PMID: 11034781]
6. Osborne, A., Thorneley, R.N., Abell, C. and Bornemann, S. Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction. J. Biol. Chem. 275 (2000) 35825-35830. [PMID: 10956653]
Accepted name: trichodiene synthase
Reaction: (2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
For reaction pathway click here.
Other name(s): trichodiene synthetase; sesquiterpene cyclase; trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase; trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 101915-76-8
References:
1. Hohn, T.M. and Vanmiddlesworth, F. Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides. Arch. Biochem. Biophys. 251 (1986) 756-761. [PMID: 3800398]
2. Hohn, T.M. and Beremand, P.D. Isolation and nucleotide sequence of a sesquiterpene cyclase gene from the trichothecene-producing fungus Fusarium sporotrichioides. Gene 79 (1989) 131-138. [PMID: 2777086]
3. Rynkiewicz, M.J., Cane, D.E. and Christianson, D.W. Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade. Proc. Natl. Acad. Sci. USA 98 (2001) 13543-13548. [PMID: 11698643]
Accepted name: pentalenene synthase
Reaction: (2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
For reaction pathway click here and mechanism click here.
Glossary: pentalenene = (1R,8aR)-1,4,7,7-tetramethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene
Other name(s): pentalenene synthetase; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, pentalenene-forming)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, pentalenene-forming)
Comments: Isolated from Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics. The 9si hydrogen of farnesyl diphosphate undergoes a 1,2-hydride shift where it becomes the 1α hydrogen of pentalenene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 90597-46-9
References:
1. Cane, D.E. Cell-free studies of monoterpene and sesquiterpene biosynthesis. Biochem. Soc. Trans. 11 (1983) 510-515. [PMID: 6642060]
2. Cane, D.E. and Tillman, A.M. Pentalenene biosynthesis and the enzymic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc. 105 (1983) 122-124.
3. Cane, D.E., Sohng, J.K., Lamberson, C.R., Rudnicki, S.M., Wu, Z., Lloyd, M.D., Oliver, J.S. and Hubbard, B.R. Pentalenene synthase. Purification, molecular cloning, sequencing, and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319. Biochemistry 33 (1994) 5846-5857. [PMID: 8180213]
Accepted name: casbene synthase
Reaction: geranylgeranyl diphosphate = casbene + diphosphate
For reaction pathway click here.
Other name(s): casbene synthetase; geranylgeranyl-diphosphate diphosphate-lyase (cyclizing)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, CASbene-forming)
Comments: The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 69106-45-2
References:
1. Moesta, P. and West, C.A. Casbene synthetase: regulation of phytoalexin biosynthesis in Ricinus communis L. seedlings. Purification of casbene synthetase and regulation of its biosynthesis during elicitation. Arch. Biochem. Biophys. 238 (1985) 325-333. [PMID: 3985625]
2. Mau, C.J. and West, C.A. Cloning of casbene synthase cDNA: evidence for conserved structural features among terpenoid cyclases in plants. Proc. Natl. Acad. Sci. USA 91 (1994) 8497-8501. [PMID: 8078910]
Accepted name: aristolochene synthase
Reaction: (2E,6E)-farnesyl diphosphate = aristolochene + diphosphate
For diagram, click here
Other name(s): sesquiterpene cyclase; trans,trans-farnesyl diphosphate aristolochene-lyase; trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming); 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming)
Comments: The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti [5] (see also EC 4.2.3.23, germacrene-A synthase). The enzyme from Penicillium roqueforti requires Mg2+. Mn2+ can partially substitute, at low concentrations. Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 94185-89-4
References:
1. Cane, D.E., Prabhakaran, P.C., Oliver, J.S. and McIlwaine, D.B. Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc. 112 (1990) 3209-3210.
2. Cane, D.E., Prabhakaran, P.C., Salaski, E.J., Harrison, P.M.H., Noguchi, H. and Rawlings, B.J. Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc. 111 (1989) 8914-8916.
3. Hohn, T.M. and Plattner, R.D. Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti. Arch. Biochem. Biophys. 272 (1989) 137-143. [PMID: 2544140]
4. Proctor, R.H. and Hohn, T.M. Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti. J. Biol. Chem. 268 (1993) 4543-4548. [PMID: 8440737]
5. Calvert, M.J., Ashton, P.R. and Allemann, R.K. Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene. J. Am. Chem. Soc. 124 (2002) 11636-11641. [PMID: 12296728]
Accepted name: (–)-endo-fenchol synthase
Reaction: geranyl diphosphate + H2O = (–)-endo-fenchol + diphosphate
For reaction 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. [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]
Accepted name: sabinene-hydrate synthase
Reaction: geranyl diphosphate + H2O = sabinene hydrate + diphosphate
For reaction 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. [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. [PMID: 2916845]
Accepted name: 6-pyruvoyltetrahydropterin synthase
Reaction: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
For diagram of reaction click here.
Glossary: 7,8-dihydroneopterin 3'-triphosphate = 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
Other name(s): 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase; 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
Systematic name: 7,8-dihydroneopterin 3'-triphosphate triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
Comments: Catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 3.5.4.16 (GTP cyclohydrolase I) [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 97089-82-2
References:
1. Milstien, S., Kaufman, S. The biosynthesis of tetrahydrobiopterin in rat brain. Purification and characterization of 6-pyruvoyl-tetrahydrobiopterin(2'-oxo) reductase. J. Biol. Chem. 264 (1989) 8066-8073. [PMID: 2656673]
2. Thöny, B., Leimbacher, W., Bürgisser, D., Heinzmann, C.W. Human 6-pyruvoyl-tetrahydrobiopterin synthase: cDNA cloning and heterologous expression of the recombinant enzyme. Biochem. Biophys. Res. Commun. 189 (1992) 1437-1443. [PMID: 1282802]
3. Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202. [PMID: 16510994]
Accepted name: (+)-δ-cadinene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (+)-δ-cadinene + diphosphate
For reaction pathway click here.
Other name(s): 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-δ-cadinene-forming)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-δ-cadinene-forming)
Comments: the sesquiterpenoid (+)-δ-cadinene is an intermediate in phytoalexin biosynthesis. Mg2+ is required for activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 166800-09-5
References:
1. Chen, X.-Y., Chen, Y., Heinstein, P., Davisson, V.J. Cloning, expression and characterization of (+)-δ-cadinene synthase: a catalyst for cotton phytoalexin biosynthesis. Arch. Biochem. Biophys. 324 (1995) 255-266. [PMID: 8554317]
2. Davis, E.M., Tsuji, J., Davis, G.D., Pierce, M.L., Essenberg, M. Purification of (+)-δ-cadinene synthase, a sesquiterpene cyclase from bacteria-inoculated cotton foliar tissue. Phytochemistry 41 (1996) 1047-1055.
3. Davis, G.D., Essenberg, M. (+)-δ-Cadinene is a product of sesquiterpene cyclase activity in cotton. Phytochemistry 39 (1995) 553-567.
[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)]
Accepted name: myrcene synthase
Reaction: geranyl diphosphate = myrcene + diphosphate
For reaction click here.
Glossary entries:
myrcene: 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. [PMID: 9268308]
Accepted name: (4S)-limonene synthase
Reaction: geranyl diphosphate = (S)-limonene + diphosphate
For diagram click here.
Glossary:
limonene = a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-(4S)-limonene synthase; 4S-(–)-limonene synthase; geranyldiphosphate diphosphate lyase (limonene forming); geranyl-diphosphate diphosphate-lyase [cyclizing, (4S)-limonene-forming]; geranyl-diphosphate 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. [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. [PMID: 8806736]
Accepted name: taxadiene synthase
Reaction: geranylgeranyl diphosphate = taxa-4,11-diene + diphosphate
For reaction pathway 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. [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. [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. [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) 185-90. [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. [PMID: 11137819]
Accepted name: abieta-7,13-diene synthase
Reaction: (+)-copalyl diphosphate = abieta-7,13-diene + diphosphate
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. [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. [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. [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. [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. [PMID: 12059223]
Accepted name: ent-kaurene synthase
Reaction: ent-copalyl diphosphate = ent-kaurene + diphosphate
For diagram of reaction, click here and mechanism here.
Other name(s): ent-kaurene synthase B; ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase (cyclizing)
Systematic name: ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-kaurene-forming)
Comments: Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9055-64-5
References:
1. Fall, R.R., West, C.A. Purification and properties of kaurene synthetase from Fusarium moniliforme. J. Biol. Chem. 246 (1971) 6913-6928. [PMID: 4331199]
2. Yamaguchi, S., Saito, T., Abe, H., Yamane, H., Murofushi, N. and Kamiya, Y. Molecular cloning and characterization of a cDNA encoding the gibberellin biosynthetic enzyme ent-kaurene synthase B from pumpkin (Cucurbita maxima L.). Plant J. 10 (1996) 203-213. [PMID: 8771778]
3. Kawaide, H., Imai, R., Sassa, T. and Kamiya, Y. Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis. J. Biol. Chem. 272 (1997) 21706-21712. [PMID: 9268298]
4. Toyomasu, T., Kawaide, H., Ishizaki, A., Shinoda, S., Otsuka, M., Mitsuhashi, W. and Sassa, T. Cloning of a full-length cDNA encoding ent-kaurene synthase from Gibberella fujikuroi: functional analysis of a bifunctional diterpene cyclase. Biosci. Biotechnol. Biochem. 64 (2000) 660-664. [PMID: 10803977]
Accepted name: (R)-limonene synthase
Reaction: geranyl diphosphate = (4R)-limonene + diphosphate
For diagram click here.
Glossary:
limonene = a monoterpenoid
(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. Lucker, J., El Tamer, M.K., Schwab, W., Verstappen, F.W., van der Plas, L.H., Bouwmeester, H.J. and Verhoeven, H.A. Monoterpene biosynthesis in lemon (Citrus limon). cDNA isolation and functional analysis of four monoterpene synthases. Eur. J. Biochem. 269 (2000) 3160-3171. [PMID: 12084056]
3. Maruyama, T., Ito, M., Kiuchi, F. and Honda, G. Molecular cloning, functional expression and characterization of d-limonene synthase from Schizonepeta tenuifolia. Biol. Pharm. Bull. 24 (2001) 373-377. [PMID: 11305598]
Accepted name: vetispiradiene synthase
Reaction: (2E,6E)-farnesyl diphosphate = vetispiradiene + diphosphate
For diagram, click here.
Other name(s): vetispiradiene-forming farnesyl pyrophosphate cyclase; pemnaspirodiene synthase; HVS; vetispiradiene cyclase; trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, vetispiradiene-forming)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, vetispiradiene-forming)
Comments: The initial internal cyclization produces the monocyclic intermediate germacrene A.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 192465-18-2
References:
1. Back, K. and Chappell, J. Cloning and bacterial expression of a sesquiterpene cyclase from Hyoscyamus muticus and its molecular comparison to related terpene cyclases. J. Biol. Chem. 270 (1995) 7375-7381. [PMID: 7706281]
2. Keller, H., Czernic, P., Ponchet, M., Ducrot, P.H., Back, K., Chappell, J., Ricci, P. and Marco, Y. Sesquiterpene cyclase is not a determining factor for elicitor- and pathogen-induced capsidiol accumulation in tobacco. Planta 205 (1998) 467-476.
3. Mathis, J.R., Back, K., Starks, C., Noel, J., Poulter, C.D. and Chappell, J. Pre-steady-state study of recombinant sesquiterpene cyclases. Biochemistry 36 (1997) 8340-8348. [PMID: 9204881]
4. Yoshioka, H., Yamada, N. and Doke, N. cDNA cloning of sesquiterpene cyclase and squalene synthase, and expression of the genes in potato tuber infected with Phytophthora infestans. Plant Cell Physiol. 40 (1999) 993-998. [PMID: 10588069]
5. Martin, V.J., Yoshikuni, Y. and Keasling, J.D. The in vivo synthesis of plant sesquiterpenes by Escherichia coli. Biotechnol. Bioeng. 75 (2001) 497-503. [PMID: 11745124]
Accepted name: germacradienol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate
For diagram of reaction click here.
Other name(s): germacradienol/germacrene-D synthase; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]
Comments: Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. Formation of (–)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. Both products are formed from a common intermediate [2]. Other enzymes produce germacrene D as the sole product using a different mechanism. The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16 geosmin synthase), a widely occurring metabolite of many streptomycetes, bacteria and fungi [2]. Also catalyses the reaction of EC 4.2.3.75, (–)-germacrene D synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 211049-88-6
References:
1. Cane, D.E. and Watt, R.M. Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 1547-1551. [PMID: 12556563]
2. He, X. and Cane, D.E. Mechanism and stereochemistry of the germacradienol/germacrene D synthase of Streptomyces coelicolor A3(2). J. Am. Chem. Soc. 126 (2004) 2678-2679. [PMID: 14995166]
3. Gust, B., Challis, G.L., Fowler, K., Kieser, T. and Chater, K.F. PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc. Natl. Acad. Sci. USA 100 (2003) 1541-1546. [PMID: 12563033]
Accepted name: germacrene-A synthase
Reaction: (2E,6E)-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate
For diagram of reaction click here.
Other name(s): germacrene A synthase; (+)-germacrene A synthase; (+)-(10R)-germacrene A synthase; GAS; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (germacrene-A-forming); 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(+)-(R)-germacrene-A-forming]
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-(R)-germacrene-A-forming]
Comments: Requires Mg2+ for activity. While germacrene A is an enzyme-bound intermediate in the biosynthesis of a number of phytoalexins, e.g. EC 4.2.3.9 (aristolochene synthase) from some species and EC 4.2.3.21 (vetispiradiene synthase), it is the sole sesquiterpenoid product formed in chicory [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 213763-55-4
References:
1. Bouwmeester, H.J., Kodde, J., Verstappen, F.W., Altug, I.G., de Kraker, J.W. and Wallaart, T.E. Isolation and characterization of two germacrene A synthase cDNA clones from chicory. Plant Physiol. 129 (2002) 134-144. [PMID: 12011345]
2. Prosser, I., Phillips, A.L., Gittings, S., Lewis, M.J., Hooper, A.M., Pickett, J.A. and Beale, M.H. (+)-(10R)-Germacrene A synthase from goldenrod, Solidago canadensis; cDNA isolation, bacterial expression and functional analysis. Phytochemistry 60 (2002) 691-702. [PMID: 12127586]
3. de Kraker, J.W., Franssen, M.C., de Groot, A., Konig, W.A. and Bouwmeester, H.J. (+)-Germacrene A biosynthesis. The committed step in the biosynthesis of bitter sesquiterpene lactones in chicory. Plant Physiol. 117 (1998) 1381-1392. [PMID: 9701594]
4. Calvert, M.J., Ashton, P.R. and Allemann, R.K. Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene. J. Am. Chem. Soc. 124 (2002) 11636-11641. [PMID: 12296728]
5. Chang, Y.J., Jin, J., Nam, H.Y. and Kim, S.U. Point mutation of (+)-germacrene A synthase from Ixeris dentata. Biotechnol. Lett. 27 (2005) 285-288. [PMID: 15834787]
Accepted name: amorpha-4,11-diene synthase
Reaction: (2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
For diagram of reaction click here and mechanism click here.
Other name(s): amorphadiene synthase; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (amorpha-4,11-diene-forming)
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. [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. [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., Konig, W.A. and Franssen, M.C. Amorpha-4,11-diene synthase catalyses the first probable step in artemisinin biosynthesis. Phytochemistry 52 (1999) 843-854. [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. [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. [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. [PMID: 16143293]
Accepted name: S-linalool synthase
Reaction: geranyl diphosphate + H2O = (3S)-linalool + diphosphate
For diagram 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 (3S)- nor (3R)-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. [PMID: 7864636]
2. Lucker, 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. [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. [PMID: 8768373]
Accepted name: R-linalool synthase
Reaction: geranyl diphosphate + H2O = (3R)-linalool + diphosphate
For diagram 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. [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. [PMID: 12176064]
Accepted name: isoprene synthase
Reaction: prenyl diphosphate = isoprene + diphosphate
For diagram of reaction click here
Glossary: isoprene = 2-methylbuta-1,3-diene
Other name(s): ISPC; ISPS
Systematic name: prenyl-diphosphate diphosphate-lyase (isoprene-forming)
Comments: Requires Mg2+ or Mn2+ for activity. This enzyme is located in the chloroplast of isoprene-emitting plants, such as poplar and aspen, and may be activitated by light-dependent changes in chloroplast pH and Mg2+ concentration [2,8].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 139172-14-8
References:
1. Silver, G.M. and Fall, R. Enzymatic synthesis of isoprene from dimethylallyl diphosphate in aspen leaf extracts. Plant Physiol. 97 (1991) 1588-1591. [PMID: 16668590]
2. Silver, G.M. and Fall, R. Characterization of aspen isoprene synthase, an enzyme responsible for leaf isoprene emission to the atmosphere. J. Biol. Chem. 270 (1995) 13010-13016. [PMID: 7768893]
3. Wildermuth, M.C. and Fall, R. Light-dependent isoprene emission (characterization of a thylakoid-bound isoprene synthase in Salix discolor chloroplasts). Plant Physiol. 112 (1996) 171-182. [PMID: 12226383]
4. Schnitzler, J.P., Arenz, R., Steinbrecher, R. and Lehming, A. Characterization of an isoprene synthase from leaves of Quercus petraea. Bot. Acta 109 (1996) 216-221.
5. Miller, B., Oschinski, C. and Zimmer, W. First isolation of an isoprene synthase gene from poplar and successful expression of the gene in Escherichia coli. Planta 213 (2001) 483-487. [PMID: 11506373]
6. Sivy, T.L., Shirk, M.C. and Fall, R. Isoprene synthase activity parallels fluctuations of isoprene release during growth of Bacillus subtilis. Biochem. Biophys. Res. Commun. 294 (2002) 71-75. [PMID: 12054742]
7. Sasaki, K., Ohara, K. and Yazaki, K. Gene expression and characterization of isoprene synthase from Populus alba. FEBS Lett. 579 (2005) 2514-2518. [PMID: 15848197]
8. Schnitzler, J.-P., Zimmer, I., Bachl, A., Arend, M., Fromm, J. and Fischbach, R.J. Biochemical properties of isoprene synthase in poplar (Populus x canescens. Planta 222 (2005) 777-786. [PMID: 16052321]
Accepted name: ent-cassa-12,15-diene synthase
Reaction: ent-copalyl diphosphate = ent-cassa-12,15-diene + diphosphate
For diagram of reaction, click here
Other name(s): OsDTC1; OsKS7
Systematic name: ent-copalyl-diphosphate diphosphate-lyase (ent-cassa-12,15-diene-forming)
Comments: This class I diterpene cyclase produces ent-cassa-12,15-diene, a precursor of the rice phytoalexins (–)-phytocassanes A-E. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Cho, E.M., Okada, A., Kenmoku, H., Otomo, K., Toyomasu, T., Mitsuhashi, W., Sassa, T., Yajima, A., Yabuta, G., Mori, K., Oikawa, H., Toshima, H., Shibuya, N., Nojiri, H., Omori, T., Nishiyama, M. and Yamane, H. Molecular cloning and characterization of a cDNA encoding ent-cassa-12,15-diene synthase, a putative diterpenoid phytoalexin biosynthetic enzyme, from suspension-cultured rice cells treated with a chitin elicitor. Plant J. 37 (2004) 1-8. [PMID: 14675427]
Accepted name: ent-sandaracopimaradiene synthase
Reaction: ent-copalyl diphosphate = ent-sandaracopimara-8(14),15-diene + diphosphate
For diagram of reaction, click here
Other name(s): OsKS10; ent-sandaracopimara-8(14),15-diene synthase
Systematic name: ent-copalyl-diphosphate diphosphate-lyase [ent-sandaracopimara-8(14),15-diene-forming]
Comments: ent-Sandaracopimaradiene is a precursor of the rice oryzalexins A-F. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation. As a minor product, this enzyme also forms ent-pimara-8(14),15-diene, which is the sole product of EC 4.2.3.30, ent-pimara-8(14),15-diene synthase. ent-Pimara-8(14),15-diene is not a precursor in the biosynthesis of either gibberellins or phytoalexins [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Otomo, K., Kanno, Y., Motegi, A., Kenmoku, H., Yamane, H., Mitsuhashi, W., Oikawa, H., Toshima, H., Itoh, H., Matsuoka, M., Sassa, T. and Toyomasu, T. Diterpene cyclases responsible for the biosynthesis of phytoalexins, momilactones A, B, and oryzalexins A-F in rice. Biosci. Biotechnol. Biochem. 68 (2004) 2001-2006. [PMID: 15388982]
2. Kanno, Y., Otomo, K., Kenmoku, H., Mitsuhashi, W., Yamane, H., Oikawa, H., Toshima, H., Matsuoka, M., Sassa, T. and Toyomasu, T. Characterization of a rice gene family encoding type-A diterpene cyclases. Biosci. Biotechnol. Biochem. 70 (2006) 1702-1710. [PMID: 16861806]
Accepted name: ent-pimara-8(14),15-diene synthase
Reaction: ent-copalyl diphosphate = ent-pimara-8(14),15-diene + diphosphate
For diagram of reaction, click here
Other name(s): OsKS5
Systematic name: ent-copalyl-diphosphate diphosphate-lyase [ent-pimara-8(14),15-diene-forming]
Comments: Unlike EC 4.2.3.29, ent-sandaracopimaradiene synthase, which can produce both ent-sandaracopimaradiene and ent-pimara-8(14),15-diene, this diterpene cyclase produces only ent-pimara-8(14),15-diene. ent-Pimara-8(14),15-diene is not a precursor in the biosynthesis of either gibberellins or phytoalexins.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kanno, Y., Otomo, K., Kenmoku, H., Mitsuhashi, W., Yamane, H., Oikawa, H., Toshima, H., Matsuoka, M., Sassa, T. and Toyomasu, T. Characterization of a rice gene family encoding type-A diterpene cyclases. Biosci. Biotechnol. Biochem. 70 (2006) 1702-1710. [PMID: 16861806]
Accepted name: ent-pimara-9(11),15-diene synthase
Reaction: ent-copalyl diphosphate = ent-pimara-9(11),15-diene + diphosphate
For diagram of reaction, click here
Other name(s): PMD synthase
Systematic name: ent-copalyl-diphosphate diphosphate-lyase [ent-pimara-9(11),15-diene-forming]
Comments: This enzyme is involved in the biosynthesis of the diterpenoid viguiepinol and requires Mg2+, Co2+, Zn2+ or Ni2+ for activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ikeda, C., Hayashi, Y., Itoh, N., Seto, H. and Dairi, T. Functional analysis of eubacterial ent-copalyl diphosphate synthase and pimara-9(11),15-diene synthase with unique primary sequences. J. Biochem. 141 (2007) 37-45. [PMID: 17148547]
Accepted name: levopimaradiene synthase
Reaction: (+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate
For diagram of reaction 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, CAS registry number:
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. [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. [PMID: 16497345]
Accepted name: stemar-13-ene synthase
Reaction: 9α-copalyl diphosphate = stemar-13-ene + diphosphate
For diagram of reaction, click here
Glossary: syn-copalyl diphosphate = 9α-copalyl diphosphate
Other name(s): OsDTC2; OsK8; OsKL8; OsKS8; stemarene synthase; syn-stemar-13-ene synthase
Systematic name: 9α-copalyl-diphosphate diphosphate-lyase (stemar-13-ene-forming)
Comments: This diterpene cyclase produces stemar-13-ene, a putative precursor of the rice phytoalexin oryzalexin S. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mohan, R.S., Yee, N.K., Coates, R.M., Ren, Y.Y., Stamenkovic, P., Mendez, I. and West, C.A. Biosynthesis of cyclic diterpene hydrocarbons in rice cell suspensions: conversion of 9,10-syn-labda-8(17),13-dienyl diphosphate to 9β-pimara-7,15-diene and stemar-13-ene. Arch. Biochem. Biophys. 330 (1996) 33-47. [PMID: 8651702]
2. Nemoto, T., Cho, E.M., Okada, A., Okada, K., Otomo, K., Kanno, Y., Toyomasu, T., Mitsuhashi, W., Sassa, T., Minami, E., Shibuya, N., Nishiyama, M., Nojiri, H. and Yamane, H. Stemar-13-ene synthase, a diterpene cyclase involved in the biosynthesis of the phytoalexin oryzalexin S in rice. FEBS Lett. 571 (2004) 182-186. [PMID: 15280039]
Accepted name: stemod-13(17)-ene synthase
Reaction: 9α-copalyl diphosphate = stemod-13(17)-ene + diphosphate
For diagram of reaction, click here
Glossary: syn-copalyl diphosphate = 9α-copalyl diphosphate
exo-stemodene = stemod-13(17)-ene
Other name(s): OsKSL11; stemodene synthase
Systematic name: 9α-copalyl-diphosphate diphosphate-lyase [stemod-13(17)-ene-forming]
Comments: This enzyme catalyses the committed step in the biosynthesis of the stemodane family of diterpenoid secondary metabolites, some of which possess mild antiviral activity. The enzyme also produces stemod-12-ene and stemar-13-ene as minor products.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Morrone, D., Jin, Y., Xu, M., Choi, S.Y., Coates, R.M. and Peters, R.J. An unexpected diterpene cyclase from rice: functional identification of a stemodene synthase. Arch. Biochem. Biophys. 448 (2006) 133-140. [PMID: 16256063]
Accepted name: syn-pimara-7,15-diene synthase
Reaction: 9α-copalyl diphosphate = 9β-pimara-7,15-diene + diphosphate
For diagram of reaction, click here
Glossary: syn-copalyl diphosphate = 9α-copalyl diphosphate
syn-pimara-7,15-diene = 9β-pimara-7,15-diene
Other name(s): 9β-pimara-7,15-diene synthase; OsDTS2; OsKS4
Systematic name: 9α-copalyl-diphosphate diphosphate-lyase (9β-pimara-7,15-diene-forming)
Comments: This enzyme is a class I terpene synthase [1]. 9β-Pimara-7,15-diene is a precursor of momilactones A and B, rice diterpenoid phytoalexins that are produced in response to attack (by a pathogen, elicitor or UV irradiation) and are involved in the defense mechanism of the plant. Momilactone B can also act as an allochemical, being constitutively produced in the root of the plant and secreted to the rhizosphere where it suppresses the growth of neighbouring plants and soil microorganisms [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wilderman, P.R., Xu, M., Jin, Y., Coates, R.M. and Peters, R.J. Identification of syn-pimara-7,15-diene synthase reveals functional clustering of terpene synthases involved in rice phytoalexin/allelochemical biosynthesis. Plant Physiol. 135 (2004) 2098-2105. [PMID: 15299118]
2. Otomo, K., Kanno, Y., Motegi, A., Kenmoku, H., Yamane, H., Mitsuhashi, W., Oikawa, H., Toshima, H., Itoh, H., Matsuoka, M., Sassa, T. and Toyomasu, T. Diterpene cyclases responsible for the biosynthesis of phytoalexins, momilactones A, B, and oryzalexins A-F in rice. Biosci. Biotechnol. Biochem. 68 (2004) 2001-2006. [PMID: 15388982]
Accepted name: terpentetriene synthase
Reaction: terpentedienyl diphosphate = terpentetriene + diphosphate
For diagram of reaction 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, CAS registry number:
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. [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. [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. [PMID: 12839434]
Accepted name: epi-isozizaene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene + diphosphate
For diagram of reaction click here and mechanism click here.
Glossary: for epi-isozizaene click here.
Other name(s): SCO5222 protein
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-epi-isozizaene-forming]
Comments: Requires Mg2+ for activity. The displacement of the diphosphate group of farnesyl diphosphate occurs with retention of configuration [1]. In the soil-dwelling bacterium Streptomyces coelicolor A3(2), the product of this reaction is used by EC 1.14.13.106, epi-isozizaene 5-monooxygenase, to produce the sesquiterpene antibiotic albaflavenone [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Lin, X., Hopson, R. and Cane, D.E. Genome mining in Streptomyces coelicolor: molecular cloning and characterization of a new sesquiterpene synthase. J. Am. Chem. Soc. 128 (2006) 6022-6023. [PMID: 16669656]
2. Zhao, B., Lin, X., Lei, L., Lamb, D.C., Kelly, S.L., Waterman, M.R. and Cane, D.E. Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2). J. Biol. Chem. 283 (2008) 8183-8189. [PMID: 18234666]
Accepted name: α-bisabolene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (E)-α-bisabolene + diphosphate
For diagram of reaction click here and mechanism 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, CAS registry number:
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. [PMID: 9618485]
Accepted name: epi-cedrol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = 8-epi-cedrol + diphosphate
For diagram of reaction click here and mechanism click here.
Other name(s): 8-epicedrol synthase; epicedrol synthase
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (8-epi-cedrol-forming)
Comments: The enzyme is activated by Mg2+ [2]. Similar to many other plant terpenoid synthases, this enzyme produces many products from a single substrate. The predominant product is the cyclic sesquiterpenoid alcohol, 8-epi-cedrol, with minor products including cedrol and the olefins α-cedrene, β-cedrene, (E)-β-farnesene and (E)-α-bisabolene [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mercke, P., Crock, J., Croteau, R. and Brodelius, P.E. Cloning, expression, and characterization of epi-cedrol synthase, a sesquiterpene cyclase from Artemisia annua L. Arch. Biochem. Biophys. 369 (1999) 213-222. [PMID: 10486140]
2. Hua, L. and Matsuda, S.P. The molecular cloning of 8-epicedrol synthase from Artemisia annua. Arch. Biochem. Biophys. 369 (1999) 208-212. [PMID: 10486139]
Accepted name: (Z)-γ-bisabolene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (Z)-γ-bisabolene + diphosphate
For diagram of reaction click here and mechanism click here.
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(Z)-γ-bisabolene-forming]
Comments: This sesquiterpenoid enzyme is constitutively expressed in the root, hydathodes and stigma of the plant Arabidopsis thaliana. If the leaves of the plant are wounded, e.g. by cutting, the enzyme is also induced close to the wound site. The sesquiterpenoids (E)-nerolidol and α-bisabolol are also produced by this enzyme as minor products.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ro, D.K., Ehlting, J., Keeling, C.I., Lin, R., Mattheus, N. and Bohlmann, J. Microarray expression profiling and functional characterization of AtTPS genes: duplicated Arabidopsis thaliana sesquiterpene synthase genes At4g13280 and At4g13300 encode root-specific and wound-inducible (Z)-γ-bisabolene synthases. Arch. Biochem. Biophys. 448 (2006) 104-116. [PMID: 16297850]
Accepted name: elisabethatriene synthase
Reaction: geranylgeranyl diphosphate = elisabethatriene + diphosphate
For reaction pathway click here and 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. [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. [PMID: 16423548]
Accepted name: aphidicolan-16β-ol synthase
Reaction: 9α-copalyl diphosphate + H2O = aphidicolan-16β-ol + diphosphate
For reaction pathway click here and mechanism click here.
Other name(s): PbACS
Systematic name: 9α-copalyl-diphosphate diphosphate-lyase (aphidicolan-16β-ol-forming)
Comment: This is a bifunctional enzyme which also has EC 5.5.1.14 syn-copalyl diphosphate synthase activity. Aphidicolan-16β-ol is a precursor of aphidicolin, a specific inhibitor of DNA polymerase α (EC 2.7.7.7).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Oikawa, H., Toyomasu, T., Toshima, H., Ohashi, S., Kawaide, H., Kamiya, Y., Ohtsuka, M., Shinoda, S., Mitsuhashi, W. and Sassa, T. Cloning and functional expression of cDNA encoding aphidicolan-16 β-ol synthase: a key enzyme responsible for formation of an unusual diterpene skeleton in biosynthesis of aphidicolin. J. Am. Chem. Soc. 123 (2001) 5154-5155. [PMID: 11457369]
2. Toyomasu, T., Nakaminami, K., Toshima, H., Mie, T., Watanabe, K., Ito, H., Matsui, H., Mitsuhashi, W., Sassa T. and Oikawa, H. Cloning of a gene cluster responsible for the biosynthesis of diterpene aphidicolin, a specific inhibitor of DNA polymerase α. Biosci. Biotechnol. Biochem. 68 (2004) 146-152. [PMID: 14745177]
Accepted name: fusicocca-2,10(14)-diene synthase
Reaction: geranylgeranyl diphosphate = fusicocca-2,10(14)-diene + diphosphate
For reaction pathway click here and mechanism click here.
Other name(s): fusicoccadiene synthase; PaFS; PaDC4
Systematic name: geranylgeranyl diphosphate-lyase (fusicocca-2,10(14)-diene-forming)
Comment: A multifunctional enzyme with EC 2.5.1.29 farnesyltranstransferase activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
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. [PMID: 17360612]
Accepted name: isopimara-7,15-diene synthase
Reaction: (+)-copalyl diphosphate = isopimara-7,15-diene + diphosphate
For reaction pathway 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)
Comment: The enzyme only gave isopimara-7,15-diene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
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. [PMID: 15310829]
Accepted name: phyllocladan-16α-ol synthase
Reaction: (+)-copalyl diphosphate + H2O = phyllocladan-16α-ol + diphosphate
For diagram of reaction click here and for mechanism 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, CAS registry number:
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. [PMID: 18391465]
Accepted name: α-farnesene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (3E,6E)-α-farnesene + diphosphate
For diagram of reaction click here.
Other name(s): (E,E)-α-farnesene synthase; AFS1; MdAFS1
Systematic name: (2E,6E)-farnesyl-diphosphate lyase [(3E,6E)-α-farnesene-forming]
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Pechous, S.W. and Whitaker, B.D. Cloning and functional expression of an (E,E)-α-farnesene synthase cDNA from peel tissue of apple fruit. Planta 219 (2004) 84-94. [PMID: 14740213]
2. Green, S., Squire, C.J., Nieuwenhuizen, N.J., Baker, E.N. and Laing, W. Defining the potassium binding region in an apple terpene synthase. J. Biol. Chem. 284 (2009) 8661-8669. [PMID: 19181671]
3. Nieuwenhuizen, N.J., Wang, M.Y., Matich, A.J., Green, S.A., Chen, X., Yauk, Y.K., Beuning, L.L., Nagegowda, D.A., Dudareva, N. and Atkinson, R.G. Two terpene synthases are responsible for the major sesquiterpenes emitted from the flowers of kiwifruit (Actinidia deliciosa). J. Exp. Bot. 60 (2009) 3203-3219. [PMID: 19516075]
Accepted name: β-farnesene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (E)-β-farnesene + diphosphate
For diagram of reaction click here.
Other name(s): farnesene synthase; terpene synthase 10; terpene synthase 10-B73; TPS10
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(E)-β-farnesene-forming]
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Zhao, B., Lei, L., Vassylyev, D.G., Lin, X., Cane, D.E., Kelly, S.L., Yuan, H., Lamb, D.C. and Waterman, M.R. Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site. J. Biol. Chem. 284 (2009) 36711-36719. [PMID: 19858213]
2. Picaud, S., Brodelius, M. and Brodelius, P.E. Expression, purification and characterization of recombinant (E)-β-farnesene synthase from Artemisia annua. Phytochemistry 66 (2005) 961-967. [PMID: 15896363]
3. Kollner, T.G., Gershenzon, J. and Degenhardt, J. Molecular and biochemical evolution of maize terpene synthase 10, an enzyme of indirect defense. Phytochemistry 70 (2009) 1139-1145. [PMID: 19646721]
4. Schnee, C., Kollner, T.G., Held, M., Turlings, T.C., Gershenzon, J. and Degenhardt, J. The products of a single maize sesquiterpene synthase form a volatile defense signal that attracts natural enemies of maize herbivores. Proc. Natl. Acad. Sci. USA 103 (2006) 1129-1134. [PMID: 16418295]
5. Maruyama, T., Ito, M. and Honda, G. Molecular cloning, functional expression and characterization of (E)-β farnesene synthase from Citrus junos. Biol. Pharm. Bull. 24 (2001) 1171-1175. [PMID: 11642326]
6. Crock, J., Wildung, M. and Croteau, R. Isolation and bacterial expression of a sesquiterpene synthase cDNA clone from peppermint (Mentha × piperita, L.) that produces the aphid alarm pheromone (E)-β-farnesene. Proc. Natl. Acad. Sci. USA 94 (1997) 12833-12838. [PMID: 9371761]
7. Schnee, C., Kollner, T.G., Gershenzon, J. and Degenhardt, J. The maize gene terpene synthase 1 encodes a sesquiterpene synthase catalyzing the formation of (E)-β-farnesene, (E)-nerolidol, and (E,E)-farnesol after herbivore damage. Plant Physiol. 130 (2002) 2049-2060. [PMID: 12481088]
8. 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. [PMID: 15921711]
Accepted name: (3S,6E)-nerolidol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (3S,6E)-nerolidol + diphosphate
For diagram of reaction click here.
Glossary: (3S,6E)-nerolidol = (3R,6E)-3,7,11-trimethyldodeca-1,6,10-trien-3-ol
Other name(s): (E)-nerolidol synthase; nerolidol synthase; (3S)-(E)-nerolidol synthase; FaNES1
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(3S,6E)-nerolidol-forming]
Comments: The enzyme catalyses a step in the formation of 4,8-dimethyl-1,3(E),7-nonatriene, a key signal molecule in induced plant defense mediated by the attraction of enemies of herbivores [2]. Nerolidol is a naturally occurring sesquiterpene found in the essential oils of many types of plants.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Aharoni, A., Giri, A.P., Verstappen, F.W., Bertea, C.M., Sevenier, R., Sun, Z., Jongsma, M.A., Schwab, W. and Bouwmeester, H.J. Gain and loss of fruit flavor compounds produced by wild and cultivated strawberry species. Plant Cell 16 (2004) 3110-3131. [PMID: 15522848]
2. Bouwmeester, H.J., Verstappen, F.W., Posthumus, M.A. and Dicke, M. Spider mite-induced (3S)-(E)-nerolidol synthase activity in cucumber and lima bean. The first dedicated step in acyclic C11-homoterpene biosynthesis. Plant Physiol. 121 (1999) 173-180. [PMID: 10482672]
3. Degenhardt, J. and Gershenzon, J. Demonstration and characterization of (E)-nerolidol synthase from maize: a herbivore-inducible terpene synthase participating in (3E)-4,8-dimethyl-1,3,7-nonatriene biosynthesis. Planta 210 (2000) 815-822. [PMID: 10805454]
4. Arimura, G., Garms, S., Maffei, M., Bossi, S., Schulze, B., Leitner, M., Mithofer, A. and Boland, W. Herbivore-induced terpenoid emission in Medicago truncatula: concerted action of jasmonate, ethylene and calcium signaling. Planta 227 (2008) 453-464. [PMID: 17924138]
Accepted name: (3R,6E)-nerolidol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (3R,6E)-nerolidol + diphosphate
For diagram of reaction click here.
Other name(s): terpene synthase 1
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(3R,6E)-nerolidol-forming]
Comments: The enzyme catalyses a step in the formation of (3E)-4,8-dimethyl-1,3,7-nonatriene, a key signal molecule in induced plant defense mediated by the attraction of enemies of herbivores [1]. Nerolidol is a naturally occurring sesquiterpene found in the essential oils of many types of plants.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Schnee, C., Kollner, T.G., Gershenzon, J. and Degenhardt, J. The maize gene terpene synthase 1 encodes a sesquiterpene synthase catalyzing the formation of (E)-β-farnesene, (E)-nerolidol, and (E,E)-farnesol after herbivore damage. Plant Physiol. 130 (2002) 2049-2060. [PMID: 12481088]
Accepted name: (+)-α-santalene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
Reaction: (2Z,6Z)-farnesyl diphosphate = (+)-α-santalene + diphosphate
For diagram of reaction click here.
Other name(s): SBS
Systematic name: (2Z,6Z)-farnesyl-diphosphate lyase (cyclizing; (+)-α-santalene-forming)
Comments: The enzyme synthesizes a mixture of sesquiterpenoids from (2Z,6Z)-farnesyl diphosphate. Following dephosphorylation of (2Z,6Z)-farnesyl diphosphate, the (2Z,6Z)-farnesyl carbocation is converted to either the (6R)- or the (6S)-bisabolyl cations depending on the stereochemistry of the 6,1 closure. The (6R)-bisabolyl cation will then lead to the formation of (+)-α-santalene, while the (6S)-bisabolyl cation will give rise to (–)-endo-α-bergamotene (see EC 4.2.3.54) and (+)-endo-β-bergamotene (see EC 4.2.3.53). Small amounts of (–)-epi-β-santalene are also formed from the (6R)-bisabolyl cation and small amounts of (–)-exo-α-bergamotene are formed from the (6S)-bisabolyl cation [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sallaud, C., Rontein, D., Onillon, S., Jabes, F., Duffe, P., Giacalone, C., Thoraval, S., Escoffier, C., Herbette, G., Leonhardt, N., Causse, M. and Tissier, A. A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites. Plant Cell 21 (2009) 301-317. [PMID: 19155349]