The Enzyme Database

Your query returned 14 entries.    printer_iconPrintable version

EC 1.14.13.207      
Transferred entry: ipsdienol synthase. Now EC 1.14.14.31, ipsdienol synthase
[EC 1.14.13.207 created 2015, deleted 2016]
 
 
EC 1.14.14.31     
Accepted name: ipsdienol synthase
Reaction: myrcene + [reduced NADPH—hemoprotein reductase] + O2 = (R)-ipsdienol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: myrcene = 7-methyl-3-methyleneocta-1,6-diene
ipsdienol = 2-methyl-6-methyleneocta-2,7-dien-4-ol
Other name(s): myrcene hydroxylase; CYP9T2; CYP9T3
Systematic name: myrcene,NADPH—hemoprotein reductase:O2 oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 heme-thiolate protein. Involved in the insect aggregation pheromone production. Isolated from the pine engraver beetle, Ips pini. A small amount of (S)-ipsdienol is also formed. In vitro it also hydroxylated (+)- and (–)-α-pinene, 3-carene, and (+)-limonene, but not α-phellandrene, (–)-β-pinene, γ-terpinene, or terpinolene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sandstrom, P., Welch, W.H., Blomquist, G.J. and Tittiger, C. Functional expression of a bark beetle cytochrome P450 that hydroxylates myrcene to ipsdienol. Insect Biochem. Mol. Biol. 36 (2006) 835–845. [DOI] [PMID: 17046597]
2.  Song, M., Kim, A.C., Gorzalski, A.J., MacLean, M., Young, S., Ginzel, M.D., Blomquist, G.J. and Tittiger, C. Functional characterization of myrcene hydroxylases from two geographically distinct Ips pini populations. Insect Biochem. Mol. Biol. 43 (2013) 336–343. [DOI] [PMID: 23376633]
[EC 1.14.14.31 created 2015 as EC 1.14.13.207, transferred 2016 to EC 1.14.14.31]
 
 
EC 4.1.99.9      
Transferred entry: myrcene synthase. Now EC 4.2.3.15, myrcene synthase
[EC 4.1.99.9 created 2000, deleted 2000]
 
 
EC 4.2.1.127     
Accepted name: linalool dehydratase
Reaction: (3S)-linalool = myrcene + H2O
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: linalool = 3,7-dimethylocta-1,6-dien-3-ol
Other name(s): linalool hydro-lyase (myrcene-forming)
Systematic name: (3S)-linalool hydro-lyase (myrcene-forming)
Comments: In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the hydration of myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol, the latter activity being classified as EC 5.4.4.4, geraniol isomerase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Brodkorb, D., Gottschall, M., Marmulla, R., Lüddeke, F. and Harder, J. Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes. J. Biol. Chem. 285 (2010) 30436–30442. [DOI] [PMID: 20663876]
2.  Lüddeke, F. and Harder, J. Enantiospecific (S)-(+)-linalool formation from β-myrcene by linalool dehydratase-isomerase. Z. Naturforsch. C 66 (2011) 409–412. [PMID: 21950166]
[EC 4.2.1.127 created 2011, modified 2012]
 
 
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.html">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 4.2.3.51     
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 4.2.3.105     
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 4.2.3.117     
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 4.2.3.119     
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 5.4.4.4     
Accepted name: geraniol isomerase
Reaction: geraniol = (3S)-linalool
For diagram of acyclic monoterpenoid biosynthesis, click here
Systematic name: geraniol hydroxymutase
Comments: In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the isomerization of (3S)-linalool to geraniol and the hydration of myrcene to (3S)-linalool, the latter activity being classified as EC 4.2.1.127, linalool dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Brodkorb, D., Gottschall, M., Marmulla, R., Lüddeke, F. and Harder, J. Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes. J. Biol. Chem. 285 (2010) 30436–30442. [DOI] [PMID: 20663876]
2.  Lüddeke, F. and Harder, J. Enantiospecific (S)-(+)-linalool formation from β-myrcene by linalool dehydratase-isomerase. Z. Naturforsch. C 66 (2011) 409–412. [PMID: 21950166]
[EC 5.4.4.4 created 2011, modified 2012]
 
 


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