Terpinolene synthase

Last updated
Terpinolene synthase
Identifiers
EC no. 4.2.3.113
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Terpinolene synthase (EC 4.2.3.113, ag9, PmeTPS2, LaLIMS_RR) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, terpinolene-forming). [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

geranyl diphosphate terpinolene + diphosphate

This enzyme requires Mg2+.

Related Research Articles

<span class="mw-page-title-main">Bornyl diphosphate synthase</span>

In enzymology, bornyl diphosphate synthase (BPPS) (EC 5.5.1.8) is an enzyme that catalyzes the chemical reaction

The enzyme (4S)-limonene synthase catalyzes the chemical reaction

The enzyme myrcene synthase catalyzes the chemical reaction

In enzymology, a pinene synthase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Juvabione</span> Chemical compound

Juvabione, historically known as the paper factor, is the methyl ester of todomatuic acid. Both are sesquiterpenes (C15) found in the wood of true firs of the genus Abies. They occur naturally as part of a mixture of sesquiterpenes based upon the bisabolane scaffold. Sesquiterpenes of this family are known as insect juvenile hormone analogues (IJHA) because of their ability to mimic juvenile activity in order to stifle insect reproduction and growth. These compounds play important roles in conifers as the second line of defense against insect induced trauma and fungal pathogens.

<span class="mw-page-title-main">Terpene synthase N terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the N terminal domain of the TPS protein.

<span class="mw-page-title-main">Terpene synthase C terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the C terminal domain of the TPS protein.

α-Bisabolene synthase (EC 4.2.3.38, bisabolene synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((E)-α-bisabolene-forming). This enzyme catalyses the following chemical reaction

β-Farnesene synthase (EC 4.2.3.47, farnesene synthase, terpene synthase 10, terpene synthase 10-B73, TPS10) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((E)-β-farnesene-forming). This enzyme catalyses the following chemical reaction

β-Phellandrene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

γ-Humulene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (γ-humulene-forming). This enzyme catalyses the following chemical reaction

(E)-γ-bisabolene synthase (EC 4.2.3.59) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((E)-γ-bisabolene-forming). This enzyme catalyses the following chemical reaction

(E)-β-Ocimene synthase (EC 4.2.3.106, β-ocimene synthase, AtTPS03, ama0a23, LjEbetaOS, MtEBOS) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase ((E)-β-ocimene-forming). This enzyme catalyses the following chemical reaction

(+)-Car-3-ene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">1,8-cineole synthase</span>

1,8-Cineole synthase (EC 4.2.3.108, 1,8-cineole cyclase, geranyl pyrophoshate:1,8-cineole cyclase, 1,8-cineole synthetase) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming). This enzyme catalyses the following chemical reaction

γ-Terpinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(–)-camphene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-camphene-forming]. This enzyme catalyses the following chemical reaction

(–)-α-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(–)-β-Pinene synthase (EC 4.2.3.120, β-geraniolene synthase, (–)-(1S,5S)-pinene synthase, geranyldiphosphate diphosphate lyase (pinene forming)) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-β-pinene-forming]. This enzyme catalyses the following chemical reaction

(+)-α-pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

References

  1. Croteau R, Satterwhite DM (September 1989). "Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (–)-pinene cyclases from sage". The Journal of Biological Chemistry. 264 (26): 15309–15. PMID   2768265.
  2. Bohlmann J, Phillips M, Ramachandiran V, Katoh S, Croteau R (August 1999). "cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis)". Archives of Biochemistry and Biophysics. 368 (2): 232–43. doi:10.1006/abbi.1999.1332. PMID   10441373.
  3. Fäldt J, Martin D, Miller B, Rawat S, Bohlmann J (January 2003). "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 Molecular Biology. 51 (1): 119–33. doi:10.1023/A:1020714403780. PMID   12602896.
  4. Huber DP, Philippe RN, Godard KA, Sturrock RN, Bohlmann J (June 2005). "Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii". Phytochemistry. 66 (12): 1427–39. doi:10.1016/j.phytochem.2005.04.030. PMID   15921711.
  5. Landmann C, Fink B, Festner M, Dregus M, Engel KH, Schwab W (September 2007). "Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia)". Archives of Biochemistry and Biophysics. 465 (2): 417–29. doi:10.1016/j.abb.2007.06.011. PMID   17662687.