The Enzyme Database

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EC 1.3.1.42     
Accepted name: 12-oxophytodienoate reductase
Reaction: (9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate + NADP+ = (9S,13S,15Z)-12-oxophyto-10,15-dienoate + NADPH + H+
Glossary: (9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate = 8-[(1S,2S)-3-oxo-2-{(Z)-pent-2-en-1-yl}cyclopentyl]octanoate
Other name(s): 12-oxo-phytodienoic acid reductase; 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+ 4-oxidoreductase; (9S,13S)-10,11-dihydro-12-oxo-15-phytoenoate:NADP+ 4-oxidoreductase; (9S,13S)-12-oxophyto-15-enoate:NADP+ 10-oxidoreductase
Systematic name: (9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate:NADP+ 10-oxidoreductase
Comments: The enzyme catalyses the reduction of (9S,13S,15Z)-12-oxophyto-10,15-dienoate during the biosynthesis of jasmonate from α-linolenate in Zea mays.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 101150-03-2
References:
1.  Vick, B.A. and Zimmerman, D.C. Characterization of 12-oxo-phytodienoic acid reductase in corn - the jasmonic acid pathway. Plant Physiol. 80 (1986) 202–205. [PMID: 16664582]
2.  Schaller, F., Biesgen, C., Mussig, C., Altmann, T. and Weiler, E.W. 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis. Planta 210 (2000) 979–984. [DOI] [PMID: 10872231]
[EC 1.3.1.42 created 1989]
 
 
EC 1.13.11.12     
Accepted name: linoleate 13S-lipoxygenase
Reaction: (1) linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
(2) α-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Other name(s): 13-lipoxidase; carotene oxidase; 13-lipoperoxidase; fat oxidase; 13-lipoxydase; lionoleate:O2 13-oxidoreductase
Systematic name: linoleate:oxygen 13-oxidoreductase
Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C-13 position with (S)-configuration. This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid. EC 1.13.11.58, linoleate 9S-lipoxygenase, catalyses a similar reaction at the second available position of these fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-60-1
References:
1.  Christopher, J., Pistorius, E. and Axelrod, B. Isolation of an enzyme of soybean lipoxidase. Biochim. Biophys. Acta 198 (1970) 12–19. [DOI] [PMID: 5461103]
2.  Theorell, H., Holman, R.T. and Åkesson, Å. Crystalline lipoxidase. Acta Chem. Scand. 1 (1947) 571–576. [PMID: 18907700]
3.  Zimmerman, D.C. Specificity of flaxseed lipoxidase. Lipids 5 (1970) 392–397. [DOI] [PMID: 5447012]
4.  Royo, J., Vancanneyt, G., Perez, A.G., Sanz, C., Stormann, K., Rosahl, S. and Sanchez-Serrano, J.J. Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns. J. Biol. Chem. 271 (1996) 21012–21019. [DOI] [PMID: 8702864]
5.  Bachmann, A., Hause, B., Maucher, H., Garbe, E., Voros, K., Weichert, H., Wasternack, C. and Feussner, I. Jasmonate-induced lipid peroxidation in barley leaves initiated by distinct 13-LOX forms of chloroplasts. Biol. Chem. 383 (2002) 1645–1657. [DOI] [PMID: 12452441]
[EC 1.13.11.12 created 1961 as EC 1.99.2.1, transferred 1965 to EC 1.13.1.13, transferred 1972 to EC 1.13.11.12, modified 2011, modified 2012]
 
 
EC 1.14.13.71      
Transferred entry: N-methylcoclaurine 3′-monooxygenase. Now EC 1.14.14.102, N-methylcoclaurine 3′-monooxygenase
[EC 1.14.13.71 created 2001, deleted 2018]
 
 
EC 1.14.13.228     
Accepted name: jasmonic acid 12-hydroxylase
Reaction: (–)-jasmonate + NADPH + H+ + O2 = trans-12-hydroxyjasmonate + NADP+ + H2O
Glossary: (–)-jasmonate = {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetate
trans-12-hydroxyjasmonate = {(1R,2R)-2-[(2Z)-5-hydroxypent-2-en-1-yl]-3-oxocyclopentyl}acetate
Other name(s): ABM (gene name)
Systematic name: jasmonate,NADPH:oxygen oxidoreductase (12-hydroxylating)
Comments: Although believed to occur in plants, the enzyme has so far been characterized only from the rice blast fungus, Magnaporthe oryzae. The fungus strategically deploys the enzyme to hydroxylate and inactivate endogenous jasmonate to evade the jasmonate-based innate immunity in rice plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Patkar, R.N., Benke, P.I., Qu, Z., Chen, Y.Y., Yang, F., Swarup, S. and Naqvi, N.I. A fungal monooxygenase-derived jasmonate attenuates host innate immunity. Nat. Chem. Biol. 11 (2015) 733–740. [DOI] [PMID: 26258762]
[EC 1.14.13.228 created 2016]
 
 
EC 1.14.14.48     
Accepted name: jasmonoyl-L-amino acid 12-hydroxylase
Reaction: a jasmonoyl-L-amino acid + [reduced NADPH—hemoprotein reductase] + O2 = a 12-hydroxyjasmonoyl-L-amino acid + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: jasmonic acid = {(1R,2R)-3-oxo-2-[(2Z)pent-2-en-1-yl]cyclopentyl}acetic acid
(+)-7-epi-jasmonic acid = {(1R,2S)-3-oxo-2-[(2Z)pent-2-en-1-yl]cyclopentyl}acetic acid
Other name(s): CYP94B1 (gene name); CYP94B3 (gene name)
Systematic name: jasmonoyl-L-amino acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P450 (heme thiolate) enzyme found in plants. The enzyme acts on jasmonoyl-L-amino acid conjugates, catalysing the hydroxylation of the C-12 position of jasmonic acid. While the best studied substrate is (+)-7-epi-jasmonoyl-L-isoleucine, the enzyme was shown to be active with jasmonoyl-L-valine and jasmonoyl-L-phenylalanine, and is likely to be active with other jasmonoyl-amino acid conjugates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Koo, A.J., Cooke, T.F. and Howe, G.A. Cytochrome P450 CYP94B3 mediates catabolism and inactivation of the plant hormone jasmonoyl-L-isoleucine. Proc. Natl. Acad. Sci. USA 108 (2011) 9298–9303. [DOI] [PMID: 21576464]
2.  Kitaoka, N., Matsubara, T., Sato, M., Takahashi, K., Wakuta, S., Kawaide, H., Matsui, H., Nabeta, K. and Matsuura, H. Arabidopsis CYP94B3 encodes jasmonyl-L-isoleucine 12-hydroxylase, a key enzyme in the oxidative catabolism of jasmonate. Plant Cell Physiol. 52 (2011) 1757–1765. [DOI] [PMID: 21849397]
3.  Heitz, T., Widemann, E., Lugan, R., Miesch, L., Ullmann, P., Desaubry, L., Holder, E., Grausem, B., Kandel, S., Miesch, M., Werck-Reichhart, D. and Pinot, F. Cytochromes P450 CYP94C1 and CYP94B3 catalyze two successive oxidation steps of plant hormone jasmonoyl-isoleucine for catabolic turnover. J. Biol. Chem. 287 (2012) 6296–6306. [DOI] [PMID: 22215670]
4.  Kitaoka, N., Kawaide, H., Amano, N., Matsubara, T., Nabeta, K., Takahashi, K. and Matsuura, H. CYP94B3 activity against jasmonic acid amino acid conjugates and the elucidation of 12-O-β-glucopyranosyl-jasmonoyl-L-isoleucine as an additional metabolite. Phytochemistry 99 (2014) 6–13. [DOI] [PMID: 24467969]
5.  Koo, A.J., Thireault, C., Zemelis, S., Poudel, A.N., Zhang, T., Kitaoka, N., Brandizzi, F., Matsuura, H. and Howe, G.A. Endoplasmic reticulum-associated inactivation of the hormone jasmonoyl-L-isoleucine by multiple members of the cytochrome P450 94 family in Arabidopsis. J. Biol. Chem. 289 (2014) 29728–29738. [DOI] [PMID: 25210037]
6.  Widemann, E., Grausem, B., Renault, H., Pineau, E., Heinrich, C., Lugan, R., Ullmann, P., Miesch, L., Aubert, Y., Miesch, M., Heitz, T. and Pinot, F. Sequential oxidation of jasmonoyl-phenylalanine and jasmonoyl-isoleucine by multiple cytochrome P450 of the CYP94 family through newly identified aldehyde intermediates. Phytochemistry 117 (2015) 388–399. [DOI] [PMID: 26164240]
[EC 1.14.14.48 created 2017]
 
 
EC 1.14.14.49     
Accepted name: 12-hydroxyjasmonoyl-L-amino acid 12-hydroxylase
Reaction: a 12-hydroxyjasmonoyl-L-amino acid + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = a 12-hydroxy-12-oxojasmonoyl-L-amino acid + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) a 12-hydroxyjasmonoyl-L-amino acid + [reduced NADPH—hemoprotein reductase] + O2 = a 12-oxojasmonoyl-L-amino acid + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1b) a 12-oxojasmonoyl-L-amino acid + [reduced NADPH—hemoprotein reductase] + O2 = a 12-hydroxy-12-oxojasmonoyl-L-amino acid + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: 12-hydroxy-12-oxojasmonate = (3Z)-5-[(1R,2R)-2-(carboxymethyl)-5-oxocyclopentyl]pent-3-enoate
Other name(s): CYP94C1 (gene name)
Systematic name: 12-hydroxyjasmonoyl-L-amino acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P450 (heme thiolate) enzyme found in plants. The enzyme acts on jasmonoyl-L-amino acid conjugates that have been hydroxylated at the C-12 position of jasmonic acid by EC 1.14.14.48, jasmonoyl-L-amino acid 12-hydroxylase, further oxidizing that position to a carboxylate via an aldehyde intermediate. While the best studied substrate is (+)-7-epi-jasmonoyl-L-isoleucine, the enzyme was shown to be active with jasmonoyl-L-phenylalanine, and is likely to be active with other jasmonoyl-amino acid conjugates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Heitz, T., Widemann, E., Lugan, R., Miesch, L., Ullmann, P., Desaubry, L., Holder, E., Grausem, B., Kandel, S., Miesch, M., Werck-Reichhart, D. and Pinot, F. Cytochromes P450 CYP94C1 and CYP94B3 catalyze two successive oxidation steps of plant hormone jasmonoyl-isoleucine for catabolic turnover. J. Biol. Chem. 287 (2012) 6296–6306. [DOI] [PMID: 22215670]
2.  Widemann, E., Grausem, B., Renault, H., Pineau, E., Heinrich, C., Lugan, R., Ullmann, P., Miesch, L., Aubert, Y., Miesch, M., Heitz, T. and Pinot, F. Sequential oxidation of jasmonoyl-phenylalanine and jasmonoyl-isoleucine by multiple cytochrome P450 of the CYP94 family through newly identified aldehyde intermediates. Phytochemistry 117 (2015) 388–399. [DOI] [PMID: 26164240]
3.  Bruckhoff, V., Haroth, S., Feussner, K., Konig, S., Brodhun, F. and Feussner, I. Functional characterization of CYP94-genes and identification of a novel jasmonate catabolite in flowers. PLoS One 11 (2016) e0159875. [DOI] [PMID: 27459369]
[EC 1.14.14.49 created 2017]
 
 
EC 1.14.14.102     
Accepted name: N-methylcoclaurine 3′-monooxygenase
Reaction: (S)-N-methylcoclaurine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-3′-hydroxy-N-methylcoclaurine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reticuline biosynthesis, click here
Other name(s): N-methylcoclaurine 3′-hydroxylase; CYP80B1 (gene name)
Systematic name: (S)-N-methylcoclaurine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzylisoquinoline alkaloid synthesis in higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 202420-37-9
References:
1.  Pauli, H.H. and Kutchan, T.M. Molecular cloning and functional heterologous expression of two alleles encoding (S)-N-methylcoclaurine 3′-hydroxylase (CYP80B1), a new methyl jasmonate-inducible cytochrome P-450-dependent mono-oxygenase of benzylisoquinoline alkaloid biosynthesis. Plant J. 13 (1998) 793–801. [DOI] [PMID: 9681018]
[EC 1.14.14.102 created 2001 as 1.14.13.71, transferred 2018 to EC 1.14.14.102]
 
 
EC 2.1.1.141     
Accepted name: jasmonate O-methyltransferase
Reaction: S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyl jasmonate
Glossary: jasmonic acid = {(1R,2R)-3-oxo-2-[(Z)pent-2-enyl]cyclopent-2-enyl}acetic acid
Other name(s): jasmonic acid carboxyl methyltransferase
Systematic name: S-adenosyl-L-methionine:jasmonate O-methyltransferase
Comments: 9,10-Dihydrojasmonic acid is a poor substrate for the enzyme. The enzyme does not convert 12-oxo-phytodienoic acid (a precursor of jasmonic acid), salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters. Enzyme activity is inhibited by the presence of divalent cations, e.g., Ca2+, Cu2+, Mg2+ and Zn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 346420-58-4
References:
1.  Seo, H.S., Song, J.T., Cheong, J.J., Lee, Y.H., Lee, Y.W., Hwang, I., Lee, J.S. and Choi, Y.D. Jasmonic acid carboxyl methyltransferase: A key enzyme for jasmonate-regulated plant responses. Proc. Natl. Acad. Sci. USA 98 (2001) 4788–4793. [DOI] [PMID: 11287667]
[EC 2.1.1.141 created 2001]
 
 
EC 2.8.2.39     
Accepted name: hydroxyjasmonate sulfotransferase
Reaction: 3′-phosphoadenylyl-sulfate + 12-hydroxyjasmonate = adenosine 3′,5′-bisphosphate + 12-sulfooxyjasmonate
Glossary: 12-hydroxyjasmonate = {(1R,2R)-2-[(2E)-5-hydroxypent-2-enyl]-3-oxocyclopentyl}acetate
Other name(s): ST2A (gene name); 3′-phosphoadenylyl-sulfate:12-hydroxyjasmonate sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:12-hydroxyjasmonate sulfonotransferase
Comments: The enzyme, charaterized from the plant Arabidopsis thaliana, also acts on 11-hydroxyjasmonate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gidda, S.K., Miersch, O., Levitin, A., Schmidt, J., Wasternack, C. and Varin, L. Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana. J. Biol. Chem. 278 (2003) 17895–17900. [DOI] [PMID: 12637544]
[EC 2.8.2.39 created 2017]
 
 
EC 3.1.1.14     
Accepted name: chlorophyllase
Reaction: chlorophyll + H2O = phytol + chlorophyllide
For diagram of chlorophyll catabolism, click here
Other name(s): CLH; Chlase
Systematic name: chlorophyll chlorophyllidohydrolase
Comments: Chlorophyllase has been found in higher plants, diatoms, and in the green algae Chlorella [3]. This enzyme forms part of the chlorophyll degradation pathway and is thought to take part in de-greening processes such as fruit ripening, leaf senescence and flowering, as well as in the turnover and homeostasis of chlorophyll [4]. This enzyme acts preferentially on chlorophyll a but will also accept chlorophyll b and pheophytins as substrates [5]. Ethylene and methyl jasmonate, which are known to accelerate senescence in many species, can enhance the activity of the hormone-inducible form of this enzyme [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-96-1
References:
1.  Holden, M. The breakdown of chlorophyll by chlorophyllase. Biochem. J. 78 (1961) 359–364. [PMID: 13715233]
2.  Klein, A.O. and Vishniac, W. Activity and partial purification of chlorophyllase in aqueous systems. J. Biol. Chem. 236 (1961) 2544–2547. [PMID: 13756631]
3.  Tsuchiya, T., Ohta, H., Okawa, K., Iwamatsu, A., Shimada, H., Masuda, T. and Takamiya, K. Cloning of chlorophyllase, the key enzyme in chlorophyll degradation: finding of a lipase motif and the induction by methyl jasmonate. Proc. Natl. Acad. Sci. USA 96 (1999) 15362–15367. [DOI] [PMID: 10611389]
4.  Okazawa, A., Tango, L., Itoh, Y., Fukusaki, E. and Kobayashi, A. Characterization and subcellular localization of chlorophyllase from Ginkgo biloba. Z. Naturforsch. [C] 61 (2006) 111–117. [PMID: 16610227]
5.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755]
[EC 3.1.1.14 created 1961, modified 2007]
 
 
EC 3.5.1.127     
Accepted name: jasmonoyl-L-amino acid hydrolase
Reaction: a jasmonoyl-L-amino acid + H2O = jasmonate + an L-amino acid
Glossary: tuberonic acid = 12-hydroxyjasmonate = {(1R,2R)-2-[(2Z)-5-hydroxypent-2-enyl]-3-oxo-cyclopentyl}acetate
jasmonate = {(1R,2R)-3-oxo-2-[(2Z)-pent-2-enyl]cyclopentyl}acetate
Other name(s): IAR3 (gene name); ILL4 (gene name); ILL6 (gene name)
Systematic name: jasmonoyl-L-amino acid amidohydrolase
Comments: This entry includes a family of enzymes that recyle jasmonoyl-amino acid conjugates back to jasmonates. The enzymes from Arabidopsis thaliana have been shown to also act on 12-hydroxyjasmonoyl-L-isoleucine, generating tuberonic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Widemann, E., Miesch, L., Lugan, R., Holder, E., Heinrich, C., Aubert, Y., Miesch, M., Pinot, F. and Heitz, T. The amidohydrolases IAR3 and ILL6 contribute to jasmonoyl-isoleucine hormone turnover and generate 12-hydroxyjasmonic acid upon wounding in Arabidopsis leaves. J. Biol. Chem. 288 (2013) 31701–31714. [DOI] [PMID: 24052260]
[EC 3.5.1.127 created 2017]
 
 
EC 4.2.1.92     
Accepted name: hydroperoxide dehydratase
Reaction: (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate = (9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
Glossary: 13-hydroperoxylinolenoate = (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
Other name(s): hydroperoxide isomerase; linoleate hydroperoxide isomerase; linoleic acid hydroperoxide isomerase; HPI; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]; allene oxide synthase; AOS
Systematic name: (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate 12,13-hydro-lyase [(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate-forming]
Comments: Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. The product of the above reaction is unstable and is acted upon by EC 5.3.99.6, allene-oxide cyclase, to form the cyclopentenone derivative (15Z)-12-oxophyto-10,15-dienoate (OPDA), which is the first cyclic and biologically active metabolite in the jasmonate biosynthesis pathway [3]. The enzyme from many plants belongs to the CYP-74 family of P-450 monooxygenases [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Esselman, W.J. and Clagett, C.O. Products of linoleic hydroperoxide-decomposing enzyme of alfalfa seed. J. Lipid Res. 15 (1974) 173–178. [PMID: 4208994]
2.  Hamberg, M. Mechanism of corn hydroperoxide isomerase - detection of 12,13(S)-oxido-9(Z),11-octadecadienoic acid. Biochim. Biophys. Acta 920 (1987) 76–84.
3.  Hamberg, M. Biosynthesis of 12-oxo-10,15(Z)-phytodienoic acid: identification of an allene oxide cyclase. Biochem. Biophys. Res. Commun. 156 (1988) 543–550. [DOI] [PMID: 3178850]
4.  Laudert, D., Pfannschmidt, U., Lottspeich, F., Holländer-Czytko, H. and Weiler, E.W. Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP 74), the first enzyme of the octadecanoid pathway to jasmonates. Plant Mol. Biol. 31 (1996) 323–335. [PMID: 8756596]
[EC 4.2.1.92 created 1992, modified 2008]
 
 
EC 4.2.3.47     
Accepted name: β-farnesene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (E)-β-farnesene + diphosphate
For diagram of acyclic sesquiterpenoid biosynthesis, 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
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15921711]
[EC 4.2.3.47 created 2010]
 
 
EC 4.2.3.48     
Accepted name: (3S,6E)-nerolidol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (3S,6E)-nerolidol + diphosphate
For diagram of acyclic sesquiterpenoid biosynthesis, 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 (3E)-4,8-dimethylnona-1,3,7-triene, 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
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 17924138]
[EC 4.2.3.48 created 2010]
 
 
EC 4.2.3.59     
Accepted name: (E)-γ-bisabolene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (E)-γ-bisabolene + diphosphate
For diagram of bisabolene biosynthesis, click here and for diagram of bisabolene biosynthesis, click here
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(E)-γ-bisabolene-forming]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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 4.2.3.59 created 2011]
 
 
EC 4.2.3.106     
Accepted name: (E)-β-ocimene synthase
Reaction: geranyl diphosphate = (E)-β-ocimene + diphosphate
Glossary: (E)-β-ocimene = (3E)-3,7-dimethylocta-1,3,6-triene
Other name(s): β-ocimene synthase; AtTPS03; ama0a23; LjEβOS; MtEBOS
Systematic name: geranyl-diphosphate diphosphate-lyase [(E)-β-ocimene-forming]
Comments: Widely distributed in plants, which release β-ocimene when attacked by herbivorous insects.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Faldt, J., Arimura, G., Gershenzon, J., Takabayashi, J. and Bohlmann, J. Functional identification of AtTPS03 as (E)-β-ocimene synthase: a monoterpene synthase catalyzing jasmonate- and wound-induced volatile formation in Arabidopsis thaliana. Planta 216 (2003) 745–751. [DOI] [PMID: 12624761]
2.  Dudareva, N., Martin, D., Kish, C.M., Kolosova, N., Gorenstein, N., Faldt, J., Miller, B. and Bohlmann, J. (E)-β-ocimene and myrcene synthase genes of floral scent biosynthesis in snapdragon: function and expression of three terpene synthase genes of a new terpene synthase subfamily. Plant Cell 15 (2003) 1227–1241. [DOI] [PMID: 12724546]
3.  Arimura, G., Ozawa, R., Kugimiya, S., Takabayashi, J. and Bohlmann, J. Herbivore-induced defense response in a model legume. Two-spotted spider mites induce emission of (E)-β-ocimene and transcript accumulation of (E)-β-ocimene synthase in Lotus japonicus. Plant Physiol. 135 (2004) 1976–1983. [DOI] [PMID: 15310830]
4.  Navia-Gine, W.G., Yuan, J.S., Mauromoustakos, A., Murphy, J.B., Chen, F. and Korth, K.L. Medicago truncatula (E)-β-ocimene synthase is induced by insect herbivory with corresponding increases in emission of volatile ocimene. Plant Physiol. Biochem. 47 (2009) 416–425. [DOI] [PMID: 19249223]
[EC 4.2.3.106 created 2012]
 
 
EC 4.2.3.107     
Accepted name: (+)-car-3-ene synthase
Reaction: geranyl diphosphate = (+)-car-3-ene + diphosphate
For diagram of monoterpenoid biosynthesis, click here
Glossary: (+)-car-3-ene = (1S,6R)-3,7,7-trimethylbicyclo[4.1.0]hept-3-ene
Other name(s): 3-carene cyclase; 3-carene synthase; 3CAR; (+)-3-carene synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]
Comments: The enzyme reacts with (3S)-linalyl diphosphate twice as rapidly as geranyl diphosphate, but 25 times as rapidly as (3R)-linalyl diphosphate. It is assumed that (3S)-linalyl diphosphate is normally formed as an enzyme bound intermediate in the reaction. In the reaction the 5-pro-R hydrogen of geranyl diphosphate is eliminated during cyclopropane ring formation [1,2]. In Picea abies (Norway spruce) and Picea sitchensis (Sitka spruce) terpinolene is also formed [4,6]. See EC 4.2.3.113 terpinolene synthase. (+)-Car-3-ene is associated with resistance of Picea sitchensis (Sitka spruce) to white pine weevil [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Savage, T.J. and Croteau, R. Biosynthesis of monoterpenes: regio- and stereochemistry of (+)-3-carene biosynthesis. Arch. Biochem. Biophys. 305 (1993) 581–587. [DOI] [PMID: 8373196]
2.  Savage, T.J., Ichii, H., Hume, S.D., Little, D.B. and Croteau, R. Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents. Arch. Biochem. Biophys. 320 (1995) 257–265. [DOI] [PMID: 7625832]
3.  Savage, T.J., Hatch, M.W. and Croteau, R. Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase. J. Biol. Chem. 269 (1994) 4012–4020. [PMID: 8307957]
4.  Faldt, J., Martin, D., Miller, B., Rawat, S. and Bohlmann, J. Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase. Plant Mol. Biol. 51 (2003) 119–133. [PMID: 12602896]
5.  Hamberger, B., Hall, D., Yuen, M., Oddy, C., Hamberger, B., Keeling, C.I., Ritland, C., Ritland, K. and Bohlmann, J. Targeted isolation, sequence assembly and characterization of two white spruce (Picea glauca) BAC clones for terpenoid synthase and cytochrome P450 genes involved in conifer defence reveal insights into a conifer genome. BMC Plant Biol. 9:106 (2009). [DOI] [PMID: 19656416]
6.  Hall, D.E., Robert, J.A., Keeling, C.I., Domanski, D., Quesada, A.L., Jancsik, S., Kuzyk, M.A., Hamberger, B., Borchers, C.H. and Bohlmann, J. An integrated genomic, proteomic and biochemical analysis of (+)-3-carene biosynthesis in Sitka spruce (Picea sitchensis) genotypes that are resistant or susceptible to white pine weevil. Plant J. 65 (2011) 936–948. [DOI] [PMID: 21323772]
[EC 4.2.3.107 created 2012]
 
 
EC 4.2.3.113     
Accepted name: terpinolene synthase
Reaction: geranyl diphosphate = terpinolene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: terpinolene = 1-methyl-4-(propan-2-ylidene)cyclohexene
Other name(s): ag9; PmeTPS2; LaLIMS_RR
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, terpinolene-forming)
Comments: Requires Mg2+. Mn2+ is less effective and product ratio changes. Forms traces of other monoterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
2.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [DOI] [PMID: 10441373]
3.  Faldt, J., Martin, D., Miller, B., Rawat, S. and Bohlmann, J. Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase. Plant Mol. Biol. 51 (2003) 119–133. [PMID: 12602896]
4.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [DOI] [PMID: 15921711]
5.  Landmann, C., Fink, B., Festner, M., Dregus, M., Engel, K.H. and Schwab, W. Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia). Arch. Biochem. Biophys. 465 (2007) 417–429. [DOI] [PMID: 17662687]
[EC 4.2.3.113 created 2012]
 
 
EC 4.2.3.117     
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 4.2.3.144     
Accepted name: geranyllinalool synthase
Reaction: geranylgeranyl diphosphate + H2O = (6E,10E)-geranyllinalool + diphosphate
For diagram of acyclic diterpenoid biosynthesis, click here
Glossary: geranylgeranyl diphosphate = (2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraen-1-yl diphosphate
(6E,10E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol
Other name(s): TPS04/GES; GES
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(E,E)-geranyllinalool-forming]
Comments: The enzyme is a component of the herbivore-induced indirect defense system. The product, (E,E)-geranyllinalool, is a precursor to the volatile compound 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT), which is released by many plants in response to damage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Herde, M., Gartner, K., Kollner, T.G., Fode, B., Boland, W., Gershenzon, J., Gatz, C. and Tholl, D. Identification and regulation of TPS04/GES, an Arabidopsis geranyllinalool synthase catalyzing the first step in the formation of the insect-induced volatile C16-homoterpene TMTT. Plant Cell 20 (2008) 1152–1168. [DOI] [PMID: 18398052]
2.  Attaran, E., Rostas, M. and Zeier, J. Pseudomonas syringae elicits emission of the terpenoid (E,E)-4,8,12-trimethyl-1,3,7,11-tridecatetraene in Arabidopsis leaves via jasmonate signaling and expression of the terpene synthase TPS4. Mol. Plant Microbe Interact. 21 (2008) 1482–1497. [DOI] [PMID: 18842097]
[EC 4.2.3.144 created 2013]
 
 
EC 6.3.2.52     
Accepted name: jasmonoyl—L-amino acid ligase
Reaction: ATP + jasmonate + an L-amino acid = AMP + diphosphate + a jasmonoyl-L-amino acid
Other name(s): JAR1 (gene name); JAR4 (gene name); JAR6 (gene name); jasmonoyl—L-amino acid synthetase
Systematic name: jasmonate:L-amino acid ligase
Comments: Two jasmonoyl-L-amino acid synthetases have been described from Nicotiana attenuata [3] and one from Arabidopsis thaliana [1]. The N. attenuata enzymes generate jasmonoyl-L-isoleucine, jasmonoyl-L-leucine, and jasmonoyl-L-valine. The enzyme from A. thaliana could catalyse the addition of many different amino acids to jasmonate in vitro [1,4,5]. While the abundant form of jasmonate in plants is (–)-jasmonate, the active form of jasmonoyl-L-isoleucine is (+)-7-iso-jasmonoyl-L-isoleucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Staswick, P.E. and Tiryaki, I. The oxylipin signal jasmonic acid is activated by an enzyme that conjugates it to isoleucine in Arabidopsis. Plant Cell 16 (2004) 2117–2127. [DOI] [PMID: 15258265]
2.  Kang, J.H., Wang, L., Giri, A. and Baldwin, I.T. Silencing threonine deaminase and JAR4 in Nicotiana attenuata impairs jasmonic acid-isoleucine-mediated defenses against Manduca sexta. Plant Cell 18 (2006) 3303–3320. [DOI] [PMID: 17085687]
3.  Wang, L., Halitschke, R., Kang, J.H., Berg, A., Harnisch, F. and Baldwin, I.T. Independently silencing two JAR family members impairs levels of trypsin proteinase inhibitors but not nicotine. Planta 226 (2007) 159–167. [DOI] [PMID: 17273867]
4.  Guranowski, A., Miersch, O., Staswick, P.E., Suza, W. and Wasternack, C. Substrate specificity and products of side-reactions catalyzed by jasmonate:amino acid synthetase (JAR1). FEBS Lett. 581 (2007) 815–820. [DOI] [PMID: 17291501]
5.  Suza, W.P. and Staswick, P.E. The role of JAR1 in jasmonoyl-L-isoleucine production during Arabidopsis wound response. Planta 227 (2008) 1221–1232. [DOI] [PMID: 18247047]
[EC 6.3.2.52 created 2018, modified 2019]
 
 


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