The Enzyme Database

Displaying entries 51-100 of 865.

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EC 2.5.1.86     Relevance: 100%
Accepted name: trans,polycis-decaprenyl diphosphate synthase
Reaction: (2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + trans,octacis-decaprenyl diphosphate
For diagram of trans,polycis-polyprenol diphosphate biosynthesis, click here
Other name(s): Rv2361c; (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase
Systematic name: (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesylcistransferase (adding 7 isopentenyl units)
Comments: The enzyme is involved in the biosynthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of essential mycobacterial cell wall components, such as the mycolyl-arabinogalactan-peptidoglycan complex and lipoarabinomannan [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kaur, D., Brennan, P.J. and Crick, D.C. Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis. J. Bacteriol. 186 (2004) 7564–7570. [DOI] [PMID: 15516568]
2.  Wang, W., Dong, C., McNeil, M., Kaur, D., Mahapatra, S., Crick, D.C. and Naismith, J.H. The structural basis of chain length control in Rv1086. J. Mol. Biol. 381 (2008) 129–140. [DOI] [PMID: 18597781]
3.  Crick, D.C., Schulbach, M.C., Zink, E.E., Macchia, M., Barontini, S., Besra, G.S. and Brennan, P.J. Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 5771–5778. [DOI] [PMID: 11004176]
[EC 2.5.1.86 created 2010]
 
 
EC 2.5.1.67     Relevance: 99.9%
Accepted name: chrysanthemyl diphosphate synthase
Reaction: 2 prenyl diphosphate = diphosphate + chrysanthemyl diphosphate
For diagram of reaction, click here
Glossary: chrysanthemyl = [2,2-dimethyl-3-(2-methylprop-1-en-1-yl)cyclopropyl]methyl
chrysanthemic acid = 2,2-dimethyl-3-(2-methylprop-1-en-1-yl)cyclopropane-1-carboxylic acid
Other name(s): CPPase; dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl-diphosphate-forming)
Systematic name: prenyl-diphosphate:prenyl-diphosphate prenyltransferase (chrysanthemyl-diphosphate-forming)
Comments: Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+ [1]. Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rivera, S.B., Swedlund, B.D., King, G.J., Bell, R.N., Hussey, C.E., Jr., Shattuck-Eidens, D.M., Wrobel, W.M., Peiser, G.D. and Poulter, C.D. Chrysanthemyl diphosphate synthase: isolation of the gene and characterization of the recombinant non-head-to-tail monoterpene synthase from Chrysanthemum cinerariaefolium. Proc. Natl. Acad. Sci. USA 98 (2001) 4373–4378. [DOI] [PMID: 11287653]
2.  Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886–6888. [DOI] [PMID: 12783539]
[EC 2.5.1.67 created 2007]
 
 
EC 2.5.1.99      
Deleted entry:  all-trans-phytoene synthase. The activity was an artifact caused by photoisomerization of the product of EC 2.5.1.32, 15-cis-phytoene synthase.
[EC 2.5.1.99 created 2012, deleted 2018]
 
 
EC 4.2.3.187     Relevance: 99.4%
Accepted name: (2Z,6E)-hedycaryol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (2Z,6E)-hedycaryol + diphosphate
For diagram of biosynthesis of ent-germacrene sesquiterpenoids, click here
Glossary: (2Z,6E)-hedycaryol = (1E,4Z,7S)-germacra-1(10),4-dien-11-ol
Other name(s): HcS
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [cyclizing, (2Z,6E)-hedycaryol-forming]
Comments: Isolated from the bacterium Kitasatospora setae. The stereochemistry suggests the farnesyl diphosphate rearranges to nerolidyl diphosphate or an equivalent intermediate before cyclization. See also EC 4.2.3.174 (2E,6E)-hedycaryol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Baer, P., Rabe, P., Citron, C.A., de Oliveira Mann, C.C., Kaufmann, N., Groll, M. and Dickschat, J.S. Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism. ChemBioChem 15 (2014) 213–216. [DOI] [PMID: 24399794]
[EC 4.2.3.187 created 2017]
 
 
EC 2.7.4.6     Relevance: 99.2%
Accepted name: nucleoside-diphosphate kinase
Reaction: ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
For diagram of GTP biosynthesis, click here
Other name(s): nucleoside 5′-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase
Systematic name: ATP:nucleoside-diphosphate phosphotransferase
Comments: Many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-51-1
References:
1.  Berg, P. and Joklik, W.K. Enzymatic phosphorylation of nucleoside diphosphates. J. Biol. Chem. 210 (1954) 657–672. [PMID: 13211603]
2.  Gibson, D.M., Ayengar, P. and Sanadi, D.R. Transphosphorylations between nucleoside phosphates. Biochim. Biophys. Acta 21 (1956) 86–91. [DOI] [PMID: 13363863]
3.  Kirkland, R.J.A. and Turner, J.F. Nucleoside diphosphokinase of pea seeds. Biochem. J. 72 (1959) 716–720. [PMID: 14409347]
4.  Krebs, H.A. and Hems, R. Some reactions of adenosine and inosine phosphates in animal tissues. Biochim. Biophys. Acta 12 (1953) 172–180. [DOI] [PMID: 13115426]
5.  Nakamura, H. and Sugino, Y. Metabolism of deoxyribonucleotides. 3. Purification and some properties of nucleoside diphosphokinase of calf thymus. J. Biol. Chem. 241 (1966) 4917–4922. [PMID: 5925862]
6.  Ratliff, R.L., Weaver, R.H., Lardy, H.A. and Kuby, S.A. Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). I. Isolation of the crystalline enzyme from brewers' yeast. J. Biol. Chem. 239 (1964) 301–309. [PMID: 14114857]
[EC 2.7.4.6 created 1961]
 
 
EC 2.5.1.81     Relevance: 98.4%
Accepted name: geranylfarnesyl diphosphate synthase
Reaction: geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): FGPP synthase; (all-E) geranylfarnesyl diphosphate synthase; GFPS; Fgs
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit)
Comments: The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate [1]. The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ogawa, T., Yoshimura, T. and Hemmi, H. Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution. Biochem. Biophys. Res. Commun. 393 (2010) 16–20. [DOI] [PMID: 20097171]
2.  Tachibana, A., Yano, Y., Otani, S., Nomura, N., Sako, Y. and Taniguchi, M. Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur. J. Biochem. 267 (2000) 321–328. [DOI] [PMID: 10632701]
3.  Tachibana, A. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett. 341 (1994) 291–294. [DOI] [PMID: 8137956]
4.  Lee, P.C., Mijts, B.N., Petri, R., Watts, K.T. and Schmidt-Dannert, C. Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. Protein Eng. Des. Sel. 17 (2004) 771–777. [DOI] [PMID: 15548566]
[EC 2.5.1.81 created 2010]
 
 
EC 4.2.3.98     Relevance: 97.9%
Accepted name: (+)-T-muurolol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (+)-T-muurolol + diphosphate
For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here
Glossary: (+)-T-muurolol = (1R,4R,4aS,8aR)-1,6-dimethyl-4-(propan-2-yl)-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-T-muurolol-forming)
Comments: The cyclization mechanism involves an intermediate nerolidyl diphosphate leading to a helminthogermacradienyl cation. After a 1,3-hydride shift of the original 1-pro-S hydrogen of farnesyl diphosphate, cyclization and deprotonation result in (+)-T-muurolol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hu, Y., Chou, W.K., Hopson, R. and Cane, D.E. Genome mining in Streptomyces clavuligerus: expression and biochemical characterization of two new cryptic sesquiterpene synthases. Chem. Biol. 18 (2011) 32–37. [DOI] [PMID: 21276937]
[EC 4.2.3.98 created 2012]
 
 
EC 4.2.3.19     Relevance: 97.8%
Accepted name: ent-kaurene synthase
Reaction: ent-copalyl diphosphate = ent-kaurene + diphosphate
For diagram of the biosynthesis of copalyl diphosphate, abietadiene and ent-kaurene, click 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 10803977]
[EC 4.2.3.19 created 2002]
 
 
EC 4.2.3.99     Relevance: 97.1%
Accepted name: labdatriene synthase
Reaction: 9α-copalyl diphosphate = (12E)-9α-labda-8(17),12,14-triene + diphosphate
For diagram of diterpenoids from 9α-copalyl diphosphate, click here
Glossary: 9α-copalyl diphosphate = syn-copalyl diphosphate = (2E)-3-methyl-5-[(1R,4aS,8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]pent-2-en-1-yl trihydrogen diphosphate
(12E)-9α-labda-8(17),12,14-triene = (4aS,5R,8aS)-1,1,4a-trimethyl-6-methylidene-5-[(2E)-3-methylpenta-2,4-dien-1-yl]decahydronaphthalene
Other name(s): OsKSL10 (gene name)
Systematic name: 9α-copalyl-diphosphate diphosphate-lyase [(12E)-9α-labda-8(17),12,14-triene-forming]
Comments: The enzyme from rice (Oryza sativa), expressed in Escherichia coli, also produces ent-sandaracopimara-8(14),15-diene from ent-copalyl diphosphate, another naturally occuring copalyl isomer in rice (cf. ent-sandaracopimaradiene synthase, EC 4.2.3.29).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morrone, D., Hillwig, M.L., Mead, M.E., Lowry, L., Fulton, D.B. and Peters, R.J. Evident and latent plasticity across the rice diterpene synthase family with potential implications for the evolution of diterpenoid metabolism in the cereals. Biochem. J. 435 (2011) 589–595. [DOI] [PMID: 21323642]
[EC 4.2.3.99 created 2012]
 
 
EC 4.2.3.188     Relevance: 97%
Accepted name: β-geranylfarnesene synthase
Reaction: (1) all-trans-geranylfarnesyl diphosphate = β-geranylfarnesene + diphosphate
(2) all-trans-hexaprenyl diphosphate = β-hexaprene + diphosphate
(3) all-trans-heptaprenyl diphosphate = β-heptaprene + diphosphate
For diagram of sesquarterpenoid biosynthesis, click here and for diagram of sesterterpenoids biosynthesis, click here
Glossary: β-geranylfarnesene = (6E,10E,14E)-7,11,15,19-tetramethyl-3-methyleneicosa-1,6,10,14,18-pentaene
Other name(s): Bcl-TS
Systematic name: all-trans-geranylfarnesyl-diphosphate diphosphate-lyase (β-geranylfarnesene-forming)
Comments: Isolated from the bacterium Bacillus clausii. The enzyme acts on a range of polyprenyl diphosphates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sato, T., Yamaga, H., Kashima, S., Murata, Y., Shinada, T., Nakano, C. and Hoshino, T. Identification of novel sesterterpene/triterpene synthase from Bacillus clausii. ChemBioChem 14 (2013) 822–825. [DOI] [PMID: 23554321]
2.  Ueda, D., Yamaga, H., Murakami, M., Totsuka, Y., Shinada, T. and Sato, T. Biosynthesis of sesterterpenes, head-to-tail triterpenes, and sesquarterpenes in Bacillus clausii: identification of multifunctional enzymes and analysis of isoprenoid metabolites. ChemBioChem 16 (2015) 1371–1377. [DOI] [PMID: 25882275]
[EC 4.2.3.188 created 2017]
 
 
EC 4.2.3.170     Relevance: 96.8%
Accepted name: 4-epi-cubebol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = 4-epi-cubebol + diphosphate
For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here
Glossary: 4-epi-cubebol = (3S,3aS,3bR,4S,7S,7aS)-4-(2-hydroxypropan-2-yl)-7-methyloctahydro-1H-cyclopenta[1,3]cyclopropa[1,2]benzen-3-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, 4-epi-cubebol-forming)
Comments: The enzyme, found in the bacterium Streptosporangium roseum, is specific for (2E,6E)-farnesyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rabe, P., Schmitz, T. and Dickschat, J.S. Mechanistic investigations on six bacterial terpene cyclases. Beilstein J. Org. Chem. 12 (2016) 1839–1850. [DOI] [PMID: 27829890]
[EC 4.2.3.170 created 2017]
 
 
EC 2.5.1.11      
Transferred entry: trans-octaprenyltranstransferase. Now covered by EC 2.5.1.84 (all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]) and EC 2.5.1.85 (all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific])
[EC 2.5.1.11 created 1972, deleted 2010]
 
 
EC 1.14.13.104      
Transferred entry: (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase
[EC 1.14.13.104 created 2008, deleted 2018]
 
 
EC 4.2.3.8     Relevance: 96.1%
Accepted name: casbene synthase
Reaction: geranylgeranyl diphosphate = casbene + diphosphate
For diagram of cembrene and related diterpenoids, 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. [DOI] [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. [DOI] [PMID: 8078910]
[EC 4.2.3.8 created 1989 as EC 4.6.1.7, transferred 2000 to EC 4.2.3.8, modified 2024]
 
 
EC 1.3.99.25     Relevance: 95.9%
Accepted name: carvone reductase
Reaction: (1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor
(2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor
For diagram of (–)-carvone catabolism, click here
Glossary: (+)-dihydrocarvone = (1S,4R)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
(–)-carvone = (4R)-mentha-1(6),8-dien-6-one = (5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-one
Systematic name: (+)-dihydrocarvone:acceptor 1,6-oxidoreductase
Comments: This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme has not been purified, and requires an unknown cofactor, which is different from NAD+, NADP+ or a flavin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [DOI] [PMID: 10832640]
[EC 1.3.99.25 created 2008]
 
 
EC 4.2.3.140     Relevance: 95.9%
Accepted name: cis-abienol synthase
Reaction: (13E)-8α-hydroxylabd-13-en-15-yl diphosphate = cis-abienol + diphosphate
For diagram of hydroxylabdenyl diphosphate derived diterpenoids, click here
Glossary: cis-abienol = (12Z)-labda-12,14-dien-8α-ol
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = 8-hydroxycopalyl diphosphate
Other name(s): Z-abienol synthase; CAS; ABS
Systematic name: (13E)-8α-hydroxylabd-13-en-15-yl-diphosphate-lyase (cis-abienol-forming)
Comments: Isolated from the plants Abies balsamea (balsam fir) [1] and Nicotiana tabacum (tobacco) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zerbe, P., Chiang, A., Yuen, M., Hamberger, B., Hamberger, B., Draper, J.A., Britton, R. and Bohlmann, J. Bifunctional cis-abienol synthase from Abies balsamea discovered by transcriptome sequencing and its implications for diterpenoid fragrance production. J. Biol. Chem. 287 (2012) 12121–12131. [DOI] [PMID: 22337889]
2.  Sallaud, C., Giacalone, C., Topfer, R., Goepfert, S., Bakaher, N., Rosti, S. and Tissier, A. Characterization of two genes for the biosynthesis of the labdane diterpene Z-abienol in tobacco (Nicotiana tabacum) glandular trichomes. Plant J. 72 (2012) 1–17. [DOI] [PMID: 22672125]
[EC 4.2.3.140 created 2012]
 
 
EC 3.6.1.76     Relevance: 95.2%
Accepted name: prenyl-diphosphate phosphatase
Reaction: (1) prenyl diphosphate + H2O = prenyl phosphate + phosphate
(2) 3-methylbut-3-en-1-yl diphosphate + H2O = 3-methylbut-3-en-1-yl phosphate + phosphate
Glossary: isopentenyl = 3-methylbut-3-en-1-yl
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl
dimethylallyl diphosphate = DMAPP
isopentenyl diphosphate = IPP
Systematic name: prenyl diphosphate/3-methylbut-3-en-1-yl diphosphate phosphohydrolase
Comments: The enzyme, characterized from the methanogenic archaeon Methanosarcina mazei, belongs to the Nudix hydrolase family (a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to a moiety). Its main purpose is to provide the substrate for EC 2.5.1.129, flavin prenyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ishibashi, Y., Matsushima, N., Ito, T. and Hemmi, H. Isopentenyl diphosphate/dimethylallyl diphosphate-specific Nudix hydrolase from the methanogenic archaeon Methanosarcina mazei. Biosci. Biotechnol. Biochem. 86 (2022) 246–253. [DOI] [PMID: 34864834]
[EC 3.6.1.76 created 2022]
 
 
EC 1.1.1.296     Relevance: 95.2%
Accepted name: dihydrocarveol dehydrogenase
Reaction: menth-8-en-2-ol + NAD+ = menth-8-en-2-one + NADH + H+
For diagram of (–)-carvone catabolism, click here
Glossary: (+)-dihydrocarveol = (1S,2S,4S)-menth-8-en-2-ol
(+)-isodihydrocarveol = (1S,2S,4R)-menth-8-en-2-ol
(+)-neoisodihydrocarveol = (1S,2R,4R)-menth-8-en-2-ol
(–)-dihydrocarvone = (1S,4S)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
Other name(s): carveol dehydrogenase (ambiguous)
Systematic name: menth-8-en-2-ol:NAD+ oxidoreductase
Comments: This enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway. The enzyme accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others. The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (–)-isodihydrocarveol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [DOI] [PMID: 10832640]
[EC 1.1.1.296 created 2008]
 
 
EC 4.2.3.116     Relevance: 95.1%
Accepted name: (+)-camphene synthase
Reaction: geranyl diphosphate = (+)-camphene + diphosphate
Glossary: (+)-camphene = (1R,4S)-2,2-dimethyl-3-methylenebicyclo[2.2.1]heptane
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-camphene-forming]
Comments: Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-camphene and (+)-α-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. Requires Mg2+ (preferred to Mn2+). See also EC 4.2.3.121 (+)-α-pinene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gambliel, H. and Croteau, R. Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration. J. Biol. Chem. 259 (1984) 740–748. [PMID: 6693393]
2.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene. J. Biol. Chem. 263 (1988) 10063–10071. [PMID: 3392006]
3.  Wagschal, K.C., Pyun, H.J., Coates, R.M. and Croteau, R. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 477–487. [DOI] [PMID: 8109978]
4.  Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [DOI] [PMID: 8109979]
[EC 4.2.3.116 created 2012]
 
 
EC 4.2.3.144     Relevance: 95%
Accepted name: geranyllinalool synthase
Reaction: geranylgeranyl diphosphate + H2O = (6E,10E)-geranyllinalool + diphosphate
For diagram of acyclic diterpenoid biosynthesis, click here
Glossary: geranylgeranyl diphosphate = (2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraen-1-yl diphosphate
(6E,10E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol
Other name(s): TPS04/GES; GES
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(E,E)-geranyllinalool-forming]
Comments: The enzyme is a component of the herbivore-induced indirect defense system. The product, (E,E)-geranyllinalool, is a precursor to the volatile compound 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT), which is released by many plants in response to damage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Herde, M., Gartner, K., Kollner, T.G., Fode, B., Boland, W., Gershenzon, J., Gatz, C. and Tholl, D. Identification and regulation of TPS04/GES, an Arabidopsis geranyllinalool synthase catalyzing the first step in the formation of the insect-induced volatile C16-homoterpene TMTT. Plant Cell 20 (2008) 1152–1168. [DOI] [PMID: 18398052]
2.  Attaran, E., Rostas, M. and Zeier, J. Pseudomonas syringae elicits emission of the terpenoid (E,E)-4,8,12-trimethyl-1,3,7,11-tridecatetraene in Arabidopsis leaves via jasmonate signaling and expression of the terpene synthase TPS4. Mol. Plant Microbe Interact. 21 (2008) 1482–1497. [DOI] [PMID: 18842097]
[EC 4.2.3.144 created 2013]
 
 
EC 4.2.3.190     Relevance: 94.9%
Accepted name: manoyl oxide synthase
Reaction: (13E)-8α-hydroxylabd-13-en-15-yl diphosphate = manoyl oxide + diphosphate
For diagram of hydroxylabdenyl diphosphate derived diterpenoids, click here
Glossary: (13E)-8α-hydroxylabd-13-en-15-yl diphosphate = 8-hydroxycopalyl diphosphate
manoyl oxide = (13R)-8,13-epoxylabd-14-ene
Other name(s): GrTPS6; CfTPS3; CfTPS4; MvELS
Systematic name: (13E)-8α-hydroxylabd-13-en-15-yl-diphosphate diphosphate-lyase (manoyl-oxide-forming)
Comments: Manoyl oxide is found in many plants. This enzyme has been isolated from the plants, Grindelia hirsutula (gum weed), Plectranthus barbatus (forskohlii) and Marrubium vulgare (white horehound).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zerbe, P., Hamberger, B., Yuen, M.M., Chiang, A., Sandhu, H.K., Madilao, L.L., Nguyen, A., Hamberger, B., Bach, S.S. and Bohlmann, J. Gene discovery of modular diterpene metabolism in nonmodel systems. Plant Physiol. 162 (2013) 1073–1091. [DOI] [PMID: 23613273]
2.  Pateraki, I., Andersen-Ranberg, J., Hamberger, B., Heskes, A.M., Martens, H.J., Zerbe, P., Bach, S.S., Moller, B.L., Bohlmann, J. and Hamberger, B. Manoyl oxide (13R), the biosynthetic precursor of forskolin, is synthesized in specialized root cork cells in Coleus forskohlii. Plant Physiol. 164 (2014) 1222–1236. [DOI] [PMID: 24481136]
3.  Zerbe, P., Chiang, A., Dullat, H., O'Neil-Johnson, M., Starks, C., Hamberger, B. and Bohlmann, J. Diterpene synthases of the biosynthetic system of medicinally active diterpenoids in Marrubium vulgare. Plant J. 79 (2014) 914–927. [DOI] [PMID: 24990389]
[EC 4.2.3.190 created 2017]
 
 
EC 4.2.3.220     Relevance: 94.7%
Accepted name: talaropentaene synthase
Reaction: all-trans-hexaprenyl diphosphate = talaropentaene + diphosphate
Glossary: talaropentaene = (3aS,5E,9E)-3a,6,10-trimethyl-1-[(2ξ,4E,8E)-undeca-5,9-dien-2-yl]-3,3a,4,7,8,11,12-octahydrocyclopenta[11]annulene
Other name(s): TvTS
Systematic name: pentaprenyl-diphosphate diphosphate-lyase [cyclizing, talaropentaene-forming]
Comments: Isolated from the fungus Talaromyces verruculosus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tao, H., Lauterbach, L., Bian, G., Chen, R., Hou, A., Mori, T., Cheng, S., Hu, B., Lu, L., Mu, X., Li, M., Adachi, N., Kawasaki, M., Moriya, T., Senda, T., Wang, X., Deng, Z., Abe, I., Dickschat, J.S. and Liu, T. Discovery of non-squalene triterpenes. Nature 606 (2022) 414–419. [DOI] [PMID: 35650436]
[EC 4.2.3.220 created 2024]
 
 
EC 4.2.3.27     Relevance: 94.6%
Accepted name: isoprene synthase
Reaction: prenyl diphosphate = isoprene + diphosphate
For diagram of isoprene biosynthesis and metabolism, click here
Glossary: isoprene = 2-methylbuta-1,3-diene
Other name(s): ISPC; ISPS; dimethylallyl-diphosphate diphosphate-lyase (isoprene-forming)
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 16052321]
[EC 4.2.3.27 created 2007]
 
 
EC 4.2.3.63     Relevance: 94.1%
Accepted name: (+)-cubenene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (+)-cubenene + diphosphate
For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-cubenene-forming]
Comments: Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nabeta, K., Kigure, K., Fujita, M., Nagoya, T., Ishikawa, T., Okuyama, H. and Takasawa, T. Bioynthesis of (+)-cubenene and (+)-epicubenol by cell-free extracts of cultured cells of Heteroscyphus planus and cyclization of [2H]farnesyl diphosphates. J. Chem. Soc., Perkin Trans. 1 (1995) 1935–1939.
2.  Nabeta, K., Fujita, M., Komuro, K., Katayama, K., and Takasawa, T. In vitro biosynthesis of cadinanes by cell-free extracts of cultured cells of Heteroscyphus planus. J. Chem. Soc., Perkin Trans. 1 (1997) 2065–2070.
[EC 4.2.3.63 created 2011]
 
 
EC 2.5.1.103     Relevance: 94%
Accepted name: presqualene diphosphate synthase
Reaction: 2 (2E,6E)-farnesyl diphosphate = presqualene diphosphate + diphosphate
For diagram of botryococcus braunii BOT22 squalene and botrycoccene biosynthesis, click here
Other name(s): SSL-1 (gene name); hpnD (gene name)
Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate-forming)
Comments: Isolated from the green alga Botryococcus braunii BOT22. Unlike EC 2.5.1.21, squalene synthase, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme. This compound is then converted into either squalene (by EC 1.3.1.96, Botryococcus squalene synthase) or botryococcene (EC 1.3.1.97, botryococcene synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Niehaus, T.D., Okada, S., Devarenne, T.P., Watt, D.S., Sviripa, V. and Chappell, J. Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii. Proc. Natl. Acad. Sci. USA 108 (2011) 12260–12265. [DOI] [PMID: 21746901]
2.  Pan, J.J., Solbiati, J.O., Ramamoorthy, G., Hillerich, B.S., Seidel, R.D., Cronan, J.E., Almo, S.C. and Poulter, C.D. Biosynthesis of squalene from farnesyl diphosphate in bacteria: three steps catalyzed by three enzymes. ACS Cent. Sci. 1 (2015) 77–82. [DOI] [PMID: 26258173]
[EC 2.5.1.103 created 2012]
 
 
EC 2.1.1.363     Relevance: 94%
Accepted name: pre-sodorifen synthase
Reaction: S-adenosyl-L-methionine + (2E,6E)-farnesyl diphosphate = S-adenosyl-L-homocysteine + pre-sodorifen diphosphate
Glossary: pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
sodorifen = (1S,2S,4R,5S,8s)-1,2,4,5,6,7,8-heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene
Other name(s): sodC (gene name)
Systematic name: (2E,6E)-farnesyl diphosphate 10-C-methyltransferase (cyclyzing, pre-sodorifen diphosphate producing)
Comments: The enzyme, characterized from the bacterium Serratia plymuthica, participates in biosynthesis of sodorifen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14): fnw139 (2016). [DOI] [PMID: 27231241]
2.  Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci. Rep. 7:862 (2017). [PMID: 28408760]
3.  von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855–11862. [PMID: 30133268]
[EC 2.1.1.363 created 2019]
 
 
EC 4.2.3.97     Relevance: 93.9%
Accepted name: (-)-δ-cadinene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (-)-δ-cadinene + diphosphate
For diagram of ent-cadinane sesquiterpenoid biosynthesis, click here
Glossary: (-)-δ-cadinene = (1R,8aS)-4,7-dimethyl-1-(propan-2-yl)-1,2,3,5,6,8a-hexahydronaphthalene
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (-)-δ-cadinene-forming)
Comments: The cyclization mechanism involves an intermediate nerolidyl diphosphate leading to a helminthogermacradienyl cation. Following a 1,3-hydride shift of the original 1-pro-S hydrogen of (2E,6E)-farnesyl diphosphate, cyclization and deprotonation gives (-)-δ-cadinene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hu, Y., Chou, W.K., Hopson, R. and Cane, D.E. Genome mining in Streptomyces clavuligerus: expression and biochemical characterization of two new cryptic sesquiterpene synthases. Chem. Biol. 18 (2011) 32–37. [DOI] [PMID: 21276937]
[EC 4.2.3.97 created 2012]
 
 
EC 2.5.1.20     Relevance: 93.6%
Accepted name: rubber cis-polyprenylcistransferase
Reaction: polycis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
For diagram of all-cis-polyprenyl diphosphate, click here
Other name(s): rubber allyltransferase; rubber transferase; isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase; cis-prenyl transferase; rubber polymerase; rubber prenyltransferase
Systematic name: polycis-polyprenyl-diphosphate:isopentenyl-diphosphate polyprenylcistransferase
Comments: Rubber particles act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-41-6
References:
1.  Archer, B.L. and Cockbain, E.G. Rubber transferase from Hevea brasiliensis latex. Methods Enzymol. 15 (1969) 476–480.
2.  McMullen, A.I. and McSweeney, G.P. The biosynthesis of rubber. Incorporation of isopentenyl pyrophosphate into purified rubber particles by a soluble latex-serum enzyme. Biochem. J. 101 (1966) 42–47. [PMID: 16742418]
[EC 2.5.1.20 created 1976]
 
 
EC 4.2.3.131     Relevance: 93.6%
Accepted name: miltiradiene synthase
Reaction: (+)-copalyl diphosphate = miltiradiene + diphosphate
For diagram of abietane diterpenoids biosynthesis, click here
Other name(s): SmMDS; SmiKSL; RoKSL
Systematic name: (+)-copalyl-diphosphate diphosphate-lyase (cyclizing, miltiradiene-forming)
Comments: Isolated from the plants Rosmarinus officinalis (rosemary) and Salvia miltiorrhiza. The enzyme from the plant Selaginella moellendorffii is mutifunctional and also catalyses EC 5.5.1.12, copalyl diphosphate synthase [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gao, W., Hillwig, M.L., Huang, L., Cui, G., Wang, X., Kong, J., Yang, B. and Peters, R.J. A functional genomics approach to tanshinone biosynthesis provides stereochemical insights. Org. Lett. 11 (2009) 5170–5173. [DOI] [PMID: 19905026]
2.  Sugai, Y., Ueno, Y., Hayashi, K., Oogami, S., Toyomasu, T., Matsumoto, S., Natsume, M., Nozaki, H. and Kawaide, H. Enzymatic 13C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii. J. Biol. Chem. 286 (2011) 42840–42847. [DOI] [PMID: 22027823]
3.  Bruckner, K., Bozic, D., Manzano, D., Papaefthimiou, D., Pateraki, I., Scheler, U., Ferrer, A., de Vos, R.C., Kanellis, A.K. and Tissier, A. Characterization of two genes for the biosynthesis of abietane-type diterpenes in rosemary (Rosmarinus officinalis) glandular trichomes. Phytochemistry 101 (2014) 52–64. [DOI] [PMID: 24569175]
[EC 4.2.3.131 created 2012]
 
 
EC 2.5.1.1     Relevance: 93.6%
Accepted name: dimethylallyltranstransferase
Reaction: prenyl diphosphate + 3-methylbut-3-en-1-yl diphosphate = diphosphate + geranyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: 3-methylbut-3-en-1-yl = isopentenyl (ambiguous)
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl (ambiguous)
Other name(s): geranyl-diphosphate synthase; prenyltransferase; dimethylallyltransferase; DMAPP:IPP-dimethylallyltransferase; (2E,6E)-farnesyl diphosphate synthetase; diprenyltransferase; geranyl pyrophosphate synthase; geranyl pyrophosphate synthetase; trans-farnesyl pyrophosphate synthetase; dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallyltranstransferase
Systematic name: prenyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate prenyltranstransferase
Comments: This enzyme will not accept larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-79-5
References:
1.  Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91–100.
2.  Sagami, H., Ogura, K., Seto, S. and Kurokawa, T. A new prenyltransferase from Micrococcus lysodeikticus. Biochem. Biophys. Res. Commun. 85 (1978) 572–578. [DOI] [PMID: 736921]
[EC 2.5.1.1 created 1961]
 
 
EC 4.2.3.213     Relevance: 93.4%
Accepted name: colleterpenol synthase
Reaction: all-trans-hexaprenyl diphosphate + H2O = colleterpenol + diphosphate
Glossary: colleterpenol = (2S)-2-[(1R,3E,7E,11E)-4,8,12-trimethylcyclotetradeca-3,7,11-trien-1-yl]undeca-5,9-dien-2-ol
Other name(s): CgCS
Systematic name: pentaprenyl-diphosphate diphosphate-lyase [cyclizing, colleterpenol-forming]
Comments: Isolated from Colletotrichum gloeosporioides, a pathogenic fungus that causes bitter rot in variety of crops.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tao, H., Lauterbach, L., Bian, G., Chen, R., Hou, A., Mori, T., Cheng, S., Hu, B., Lu, L., Mu, X., Li, M., Adachi, N., Kawasaki, M., Moriya, T., Senda, T., Wang, X., Deng, Z., Abe, I., Dickschat, J.S. and Liu, T. Discovery of non-squalene triterpenes. Nature 606 (2022) 414–419. [DOI] [PMID: 35650436]
[EC 4.2.3.213 created 2023]
 
 
EC 4.2.3.11     Relevance: 93%
Accepted name: sabinene-hydrate synthase
Reaction: geranyl diphosphate + H2O = sabinene hydrate + diphosphate
For diagram of monoterpenoid biosynthesis, click here
Other name(s): sabinene hydrate cyclase
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, sabinene-hydrate-forming)
Comments: Both cis- and trans- isomers of sabinene hydrate are formed. (3R)-Linalyl diphosphate is an intermediate in the reaction
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117164-95-1
References:
1.  Hallahan, T.W. and Croteau, R. Monoterpene biosynthesis: demonstration of a geranyl pyrophosphate:sabinene hydrate cyclase in soluble enzyme preparations from sweet marjoram (Majorana hortensis). Arch. Biochem. Biophys. 264 (1988) 618–631. [DOI] [PMID: 3401015]
2.  Hallahan, T.W. and Croteau, R. Monoterpene biosynthesis: mechanism and stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and (+)-trans-sabinene hydrate. Arch. Biochem. Biophys. 269 (1989) 313–326. [DOI] [PMID: 2916845]
[EC 4.2.3.11 created 1992 as EC 4.6.1.9, transferred 2000 to EC 4.2.3.11]
 
 
EC 4.2.3.115     Relevance: 93%
Accepted name: α-terpinene synthase
Reaction: geranyl diphosphate = α-terpinene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: α-terpinene = 1-isopropyl-4-methylcyclohexa-1,3-diene
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, α-terpinene-forming)
Comments: The enzyme has been characterized from Dysphania ambrosioides (American wormseed). Requires Mg2+. Mn2+ is less effective. The enzyme will also use (3R)-linalyl diphosphate. The reaction involves a 1,2-hydride shift. The 1-pro-S hydrogen of geranyl diphosphate is lost.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Poulose, A.J. and Croteau, R. γ-Terpinene synthetase: a key enzyme in the biosynthesis of aromatic monoterpenes. Arch. Biochem. Biophys. 191 (1978) 400–411. [DOI] [PMID: 736574]
2.  LaFever, R.E. and Croteau, R. Hydride shifts in the biosynthesis of the p-menthane monoterpenes α-terpinene, γ-terpinene, and β-phellandrene. Arch. Biochem. Biophys. 301 (1993) 361–366. [DOI] [PMID: 8460944]
[EC 4.2.3.115 created 2012]
 
 
EC 4.2.3.145     Relevance: 93%
Accepted name: ophiobolin F synthase
Reaction: (2E,6E,10E,14E)-geranylfarnesyl diphosphate + H2O = ophiobolin F + diphosphate
For diagram of biosynthesis of diterpenoids from ent-copalyl diphosphate, click here and for diagram of sesterterpenoids biosynthesis, click here
Systematic name: (2E,6E,10E,14E)-geranylfarnesyl-diphosphate diphosphate-lyase (cyclizing, ophiobolin-F-forming)
Comments: Isolated from the fungus Aspergillus clavatus. The product is a sesterterpenoid (C25 terpenoid).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chiba, R., Minami, A., Gomi, K. and Oikawa, H. Identification of ophiobolin F synthase by a genome mining approach: a sesterterpene synthase from Aspergillus clavatus. Org. Lett. 15 (2013) 594–597. [DOI] [PMID: 23324037]
[EC 4.2.3.145 created 2014]
 
 
EC 4.2.3.34     Relevance: 93%
Accepted name: stemod-13(17)-ene synthase
Reaction: 9α-copalyl diphosphate = stemod-13(17)-ene + diphosphate
For diagram of the biosynthesis of diterpenoids from 9alpha-copalyl diphosphate, 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
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. [DOI] [PMID: 16256063]
[EC 4.2.3.34 created 2008]
 
 
EC 5.5.1.13     Relevance: 93%
Accepted name: ent-copalyl diphosphate synthase
Reaction: geranylgeranyl diphosphate = ent-copalyl diphosphate
For diagram of biosynthesis of diterpenoids from ent-copalyl diphosphate, click here
Other name(s): ent-kaurene synthase A; ent-kaurene synthetase A; ent-CDP synthase; ent-copalyl-diphosphate lyase (decyclizing)
Systematic name: ent-copalyl-diphosphate lyase (ring-opening)
Comments: Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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.  Sun, T.P. and Kamiya, Y. The Arabidopsis GA1 locus encodes the cyclase ent-kaurene synthetase A of gibberellin biosynthesis. Plant Cell 6 (1994) 1509–1518. [PMID: 7994182]
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. [DOI] [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. [DOI] [PMID: 10803977]
[EC 5.5.1.13 created 2002]
 
 
EC 2.5.1.112     Relevance: 92.9%
Accepted name: adenylate dimethylallyltransferase (ADP/ATP-dependent)
Reaction: (1) prenyl diphosphate + ADP = diphosphate + N6-prenyladenosine 5′-diphosphate
(2) prenyl diphosphate + ATP = diphosphate + N6-prenyladenosine 5′-triphosphate
For diagram of N6-(Dimethylallyl)adenosine phosphates biosynthesis, click here
Other name(s): cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:ADP/ATP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); dimethylallyl diphosphate:ATP/ADP isopentenyltransferase: IPT; dimethylallyl-diphosphate:ADP/ATP dimethylallyltransferase
Systematic name: prenyl-diphosphate:ADP/ATP prenyltransferase
Comments: Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP [1]. Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus [3], also have a lower activity with AMP (cf. EC 2.5.1.27, adenylate dimethylallyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kakimoto, T. Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate:ATP/ADP isopentenyltransferases. Plant Cell Physiol. 42 (2001) 677–685. [PMID: 11479373]
2.  Takei, K., Sakakibara, H. and Sugiyama, T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 26405–26410. [DOI] [PMID: 11313355]
3.  Sakano, Y., Okada, Y., Matsunaga, A., Suwama, T., Kaneko, T., Ito, K., Noguchi, H. and Abe, I. Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.). Phytochemistry 65 (2004) 2439–2446. [DOI] [PMID: 15381407]
[EC 2.5.1.112 created 2013]
 
 
EC 4.2.3.25     Relevance: 92.9%
Accepted name: S-linalool synthase
Reaction: geranyl diphosphate + H2O = (3S)-linalool + diphosphate
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: (3S)-linalool = (3S)-3,7-dimethylocta-1,6-dien-3-ol
Other name(s): LIS; Lis; 3S-linalool synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [(3S)-linalool-forming]
Comments: Requires Mn2+ or Mg2+ for activity. Neither (S)- nor (R)-linalyl diphosphate can act as substrate for the enzyme from the flower Clarkia breweri [1]. Unlike many other monoterpene synthases, only a single product, (3S)-linalool, is formed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 160477-81-6
References:
1.  Pichersky, E., Lewinsohn, E. and Croteau, R. Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri. Arch. Biochem. Biophys. 316 (1995) 803–807. [DOI] [PMID: 7864636]
2.  Lücker, J., Bouwmeester, H.J., Schwab, W., Blaas, J., van der Plas, L.H. and Verhoeven, H.A. Expression of Clarkia S-linalool synthase in transgenic petunia plants results in the accumulation of S-linalyl-β-D-glucopyranoside. Plant J. 27 (2001) 315–324. [DOI] [PMID: 11532177]
3.  Dudareva, N., Cseke, L., Blanc, V.M. and Pichersky, E. Evolution of floral scent in Clarkia: novel patterns of S-linalool synthase gene expression in the C. breweri flower. Plant Cell 8 (1996) 1137–1148. [DOI] [PMID: 8768373]
[EC 4.2.3.25 created 2006]
 
 
EC 4.2.3.37     Relevance: 92.7%
Accepted name: epi-isozizaene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene + diphosphate
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
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. [DOI] [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. [DOI] [PMID: 18234666]
[EC 4.2.3.37 created 2008]
 
 
EC 3.1.7.5     Relevance: 92.7%
Accepted name: geranylgeranyl diphosphate diphosphatase
Reaction: geranylgeranyl diphosphate + H2O = geranylgeraniol + diphosphate
For diagram of acyclic diterpenoid biosynthesis, click here
Glossary: plaunotol = 18-hydroxygeranylgeraniol
Other name(s): geranylgeranyl diphosphate phosphatase
Systematic name: geranyl-diphosphate diphosphohydrolase
Comments: Involved in the biosynthesis of plaunotol. There are two isoenzymes with different ion requirements. Neither require Mg2+ but in addition PII is inhibited by Zn2+, Mn2+ and Co2+. It is not known which isoenzyme is involved in plaunotol biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nualkaew, N., De-Eknamkul, W., Kutchan, T.M. and Zenk, M.H. Membrane-bound geranylgeranyl diphosphate phosphatases: purification and characterization from Croton stellatopilosus leaves. Phytochemistry 67 (2006) 1613–1620. [DOI] [PMID: 16445953]
[EC 3.1.7.5 created 2009]
 
 
EC 4.2.3.205     Relevance: 92.6%
Accepted name: sodorifen synthase
Reaction: pre-sodorifen diphosphate = sodorifen + diphosphate
Glossary: pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
sodorifen = (1S,2R,8S)-1,2,4,5,6,7,8-Heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene
Other name(s): sodD (gene name)
Systematic name: pre-sodorifen diphosphate-lyase [sodorifen-forming]
Comments: The enzyme has been characterized from the bacterium Serratia plymuthica.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14): fnw139 (2016). [DOI] [PMID: 27231241]
2.  Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci. Rep. 7:862 (2017). [PMID: 28408760]
3.  von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855–11862. [PMID: 30133268]
[EC 4.2.3.205 created 2019]
 
 
EC 4.2.3.71     Relevance: 92.5%
Accepted name: (E,E)-germacrene B synthase
Reaction: (2E,6E)-farnesyl diphosphate = (E,E)-germacrene B + diphosphate
For diagram of germacrene-derived sesquiterpenoid biosynthesis, click here
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(E,E)-germacrene-B-forming]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  van Der Hoeven, R.S., Monforte, A.J., Breeden, D., Tanksley, S.D. and Steffens, J.C. Genetic control and evolution of sesquiterpene biosynthesis in Lycopersicon esculentum and L. hirsutum. Plant Cell 12 (2000) 2283–2294. [PMID: 11090225]
[EC 4.2.3.71 created 2011]
 
 
EC 4.2.3.60     Relevance: 92.5%
Accepted name: germacrene C synthase
Reaction: (2E,6E)-farnesyl diphosphate = germacrene C + diphosphate
For diagram of germacrene-derived sesquiterpenoid biosynthesis, click here
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (germacrene-C-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Colby, S.M., Crock, J., Dowdle-Rizzo, B., Lemaux, P.G. and Croteau, R. Germacrene C synthase from Lycopersicon esculentum cv. VFNT cherry tomato: cDNA isolation, characterization, and bacterial expression of the multiple product sesquiterpene cyclase. Proc. Natl. Acad. Sci. USA 95 (1998) 2216–2221. [DOI] [PMID: 9482865]
[EC 4.2.3.60 created 2011]
 
 
EC 4.2.3.169     Relevance: 92.4%
Accepted name: 7-epi-α-eudesmol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = 7-epi-α-eudesmol + diphosphate
For diagram of eudesmol and selinene biosynthesis, click here
Glossary: 7-epi-α-eudesmol = 2-[(2S,4aR,8aR)-4a,8-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalen-2-yl]propan-2-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, 7-epi-α-eudesmol-forming)
Comments: The enzyme, found in the bacterium Streptomyces viridochromogenes, is specific for (2E,6E)-farnesyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rabe, P., Schmitz, T. and Dickschat, J.S. Mechanistic investigations on six bacterial terpene cyclases. Beilstein J. Org. Chem. 12 (2016) 1839–1850. [DOI] [PMID: 27829890]
[EC 4.2.3.169 created 2017]
 
 
EC 4.2.3.166     Relevance: 92.2%
Accepted name: (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol + diphosphate
For diagram of biosynthesis of ent-germacrene sesquiterpenoids, click here
Glossary: (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol = (1S,2E,6E,10R)-3,7-dimethyl-10-(propan-2-yl)cyclodeca-2,6-dien-1-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [cyclizing, (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol-forming]
Comments: The enzyme has been identified in the bacterium Streptomyces pratensis. It is specific for (2E,6E)-farnesyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rabe, P., Barra, L., Rinkel, J., Riclea, R., Citron, C.A., Klapschinski, T.A., Janusko, A. and Dickschat, J.S. Conformational analysis, thermal rearrangement, and EI-MS fragmentation mechanism of ((1(10)E,4E,6S,7R)-germacradien-6-ol by 13C-labeling experiments. Angew. Chem. Int. Ed. Engl. 54 (2015) 13448–13451. [DOI] [PMID: 26361082]
[EC 4.2.3.166 created 2017]
 
 
EC 1.23.1.3     Relevance: 92%
Accepted name: (–)-pinoresinol reductase
Reaction: (–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+
For diagram of (–)-lariciresinol biosynthesis, click here
Glossary: (–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR
Systematic name: (–)-lariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995]
2.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599]
3.  Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [DOI] [PMID: 18347017]
[EC 1.23.1.3 created 2013]
 
 
EC 3.1.7.8      
Transferred entry: tuberculosinol synthase. Now known to be partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase.
[EC 3.1.7.8 created 2011, deleted 2020]
 
 
EC 2.5.1.153     Relevance: 91.8%
Accepted name: adenosine tuberculosinyltransferase
Reaction: tuberculosinyl diphosphate + adenosine = 1-tuberculosinyladenosine + diphosphate
Glossary: tuberculosinyl diphosphate = halima-5,13-dien-15-yl diphosphate
Other name(s): Rv3378c (locus name)
Systematic name: tuberculosinyl-diphosphate:adenosine tuberculosinyltransferase
Comments: The enzyme, characterized from the bacterial pathogen Mycobacterium tuberculosis, produces 1-tuberculosinyladenosine, an unusual terpene nucleoside that acts as a phagolysosome disruptor by neutralizing the pH, resulting in swelling of the lysosome and obliteration of its multilamellar structure.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Layre, E., Lee, H.J., Young, D.C., Martinot, A.J., Buter, J., Minnaard, A.J., Annand, J.W., Fortune, S.M., Snider, B.B., Matsunaga, I., Rubin, E.J., Alber, T. and Moody, D.B. Molecular profiling of Mycobacterium tuberculosis identifies tuberculosinyl nucleoside products of the virulence-associated enzyme Rv3378c. Proc. Natl. Acad. Sci. USA 111 (2014) 2978–2983. [DOI] [PMID: 24516143]
2.  Young, D.C., Layre, E., Pan, S.J., Tapley, A., Adamson, J., Seshadri, C., Wu, Z., Buter, J., Minnaard, A.J., Coscolla, M., Gagneux, S., Copin, R., Ernst, J.D., Bishai, W.R., Snider, B.B. and Moody, D.B. In vivo biosynthesis of terpene nucleosides provides unique chemical markers of Mycobacterium tuberculosis infection. Chem. Biol. 22 (2015) 516–526. [DOI] [PMID: 25910243]
3.  Buter, J., Cheng, T.Y., Ghanem, M., Grootemaat, A.E., Raman, S., Feng, X., Plantijn, A.R., Ennis, T., Wang, J., Cotton, R.N., Layre, E., Ramnarine, A.K., Mayfield, J.A., Young, D.C., Jezek Martinot, A., Siddiqi, N., Wakabayashi, S., Botella, H., Calderon, R., Murray, M., Ehrt, S., Snider, B.B., Reed, M.B., Oldfield, E., Tan, S., Rubin, E.J., Behr, M.A., van der Wel, N.N., Minnaard, A.J. and Moody, D.B. Mycobacterium tuberculosis releases an antacid that remodels phagosomes. Nat. Chem. Biol. 15 (2019) 889–899. [DOI] [PMID: 31427817]
[EC 2.5.1.153 created 2011 as EC 3.1.7.8 and EC 3.1.7.9, transferred 2020 to EC 2.5.1.153]
 
 
EC 4.2.3.108     Relevance: 91.8%
Accepted name: 1,8-cineole synthase
Reaction: geranyl diphosphate + H2O = 1,8-cineole + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
Other name(s): 1,8-cineole cyclase; geranyl pyrophoshate:1,8-cineole cyclase; 1,8-cineole synthetase
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming)
Comments: Requires Mn2+ or Zn2+. Mg2+ is less effective than either. 1,8-Cineole is the main product from the enzyme with just traces of other monoterpenoids. The oxygen atom is derived from water. The reaction proceeds via linalyl diphosphate and α-terpineol, the stereochemistry of both depends on the organism. However neither intermediate can substitute for geranyl diphosphate. The reaction in Salvia officinalis (sage) proceeds via (–)-(3R)-linalyl diphosphate [1-3] while that in Arabidopsis (rock cress) proceeds via (+)-(3S)-linalyl diphosphate [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 110637-19-9
References:
1.  Croteau, R., Alonso, W.R., Koepp, A.E. and Johnson, M.A. Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase. Arch. Biochem. Biophys. 309 (1994) 184–192. [DOI] [PMID: 8117108]
2.  Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J. Biol. Chem. 273 (1998) 14891–14899. [DOI] [PMID: 9614092]
3.  Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [DOI] [PMID: 12941302]
4.  Chen, F., Ro, D.K., Petri, J., Gershenzon, J., Bohlmann, J., Pichersky, E. and Tholl, D. Characterization of a root-specific Arabidopsis terpene synthase responsible for the formation of the volatile monoterpene 1,8-cineole. Plant Physiol. 135 (2004) 1956–1966. [DOI] [PMID: 15299125]
5.  Keszei, A., Brubaker, C.L., Carter, R., Kollner, T., Degenhardt, J. and Foley, W.J. Functional and evolutionary relationships between terpene synthases from Australian Myrtaceae. Phytochemistry 71 (2010) 844–852. [DOI] [PMID: 20399476]
[EC 4.2.3.108 created 2012]
 
 
EC 4.2.3.75     Relevance: 91.8%
Accepted name: (-)-germacrene D synthase
Reaction: (2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate
For diagram of gurjunene, patchoulol and selinene biosynthesis, click here
Glossary: (-)-germacrene D = (1E,6E,8S)-1-methyl-5-methylidene-8-(propan-2-yl)cyclodeca-1,6-diene
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(-)-germacrene-D-forming]
Comments: In Solidago canadensis the biosynthesis results in the pro-R hydrogen at C-1 of the farnesy diphosphate ending up at C-11 of the (-)-germacrene D [1]. With Streptomyces coelicolor the pro-S hydrogen at C-1 ends up at C-11 of the (-)-germacrene D [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schmidt, C.O., Bouwmeester, H.J., Franke, S. and König, W.A. Mechanisms of the biosynthesis of sesquiterpene enantiomers (+)- and (-)-germacrene D in Solidago canadensis. Chirality 11 (1999) 353–362.
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. [DOI] [PMID: 14995166]
3.  Lucker, J., Bowen, P. and Bohlmann, J. Vitis vinifera terpenoid cyclases: functional identification of two sesquiterpene synthase cDNAs encoding (+)-valencene synthase and (-)-germacrene D synthase and expression of mono- and sesquiterpene synthases in grapevine flowers and berries. Phytochemistry 65 (2004) 2649–2659. [DOI] [PMID: 15464152]
4.  Prosser, I., Altug, I.G., Phillips, A.L., Konig, W.A., Bouwmeester, H.J. and Beale, M.H. Enantiospecific (+)- and (-)-germacrene D synthases, cloned from goldenrod, reveal a functionally active variant of the universal isoprenoid-biosynthesis aspartate-rich motif. Arch. Biochem. Biophys. 432 (2004) 136–144. [DOI] [PMID: 15542052]
[EC 4.2.3.75 created 2011]
 
 


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