5-epiaristolochene synthase

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5-epiaristolochene synthase
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EC no. 4.2.3.61
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5-Epiaristolochene synthase (EC 4.2.3.61, 5-epi-aristolochene synthase, tobacco epiaristolochene synthase, farnesyl pyrophosphate cyclase, EAS, TEAS) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((+)-5-epiaristolochene-forming). [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate (+)-5-epiaristolochene + diphosphate

Initial cyclization gives (+)-germacrene A in an enzyme-bound form.

Related Research Articles

The enzyme aristolochene synthase catalyzes the chemical reaction

The enzyme germacrene-A synthase (EC 4.2.3.23) catalyzes the chemical reaction

The enzyme pentalenene synthase catalyzes the chemical reaction

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

Capsidiol is a terpenoid compound that accumulates in tobacco Nicotiana tabacum and chili pepper Capsicum annuum in response to fungal infection. Capsidiol is categorized under the broad term of phytoalexin, a class of low molecular weight plant secondary metabolites that are produced during infection. Phytoalexins are also characterized as a part of a two pronged response to infection which involves a short term response consisting of production of free radicals near the site of infection and a long term response involving the production of hormones and an increase in enzymes to biosynthesize phytoalexins such as capsidiol.

<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.

5-epiaristolochene 1,3-dihydroxylase (EC 1.14.13.119, 5-epi-aristolochene 1,3-dihydroxylase, EAH) is an enzyme with systematic name 5-epiaristolochene,NADPH:oxygen oxidoreductase (1- and 3-hydroxylating). This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl-diphosphate diphosphate-lyase may refer to:

epi-Cedrol synthase (EC 4.2.3.39, 8-epicedrol synthase, epicedrol synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (8-epi-cedrol-forming). 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

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

Patchoulol synthase (EC 4.2.3.70) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming). This enzyme catalyses the following chemical reaction

Valencene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (valencene-forming). It is a terpene cyclase enzyme responsible for the biosynthesis of valencene, a sesquiterpene, using farnesyl pyrophosphate as its substrate. The first such enzyme was isolated using orange cDNA. This enzyme catalyses the following chemical reaction

(–)-Germacrene D synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -germacrene-D-forming). This enzyme catalyses the following chemical reaction

(+)-δ-Selinene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -δ-selinene-forming). This enzyme catalyses the following chemical reaction

(+)-Germacrene D synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -germacrene-D-forming). This enzyme catalyses the following chemical reaction

7-epi-α-Selinene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (7-epi-α-selinene-forming). This enzyme catalyses the following chemical reaction

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

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

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

References

  1. ↑ Back K, Yin S, Chappell J (December 1994). "Expression of a plant sesquiterpene cyclase gene in Escherichia coli". Archives of Biochemistry and Biophysics. 315 (2): 527–32. doi:10.1006/abbi.1994.1533. PMID   7986100.
  2. ↑ Starks CM, Back K, Chappell J, Noel JP (September 1997). "Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase" (PDF). Science. 277 (5333): 1815–20. doi:10.1126/science.277.5333.1815. PMID   9295271. S2CID   40862740. Archived from the original (PDF) on 2020-02-07.
  3. ↑ Back K, He S, Kim KU, Shin DH (September 1998). "Cloning and bacterial expression of sesquiterpene cyclase, a key branch point enzyme for the synthesis of sesquiterpenoid phytoalexin capsidiol in UV-challenged leaves of Capsicum annuum". Plant & Cell Physiology. 39 (9): 899–904. doi: 10.1093/oxfordjournals.pcp.a029452 . PMID   9816674.
  4. ↑ Rising KA, Starks CM, Noel JP, Chappell J (2000). "Demonstration of germacrene A as an intermediate in 5-epi-aristolochene synthase catalysis". J. Am. Chem. Soc. 122 (9): 1861–1866. doi:10.1021/ja993584h.
  5. ↑ Bohlmann J, Stauber EJ, Krock B, Oldham NJ, Gershenzon J, Baldwin IT (May 2002). "Gene expression of 5-epi-aristolochene synthase and formation of capsidiol in roots of Nicotiana attenuata and N. sylvestris". Phytochemistry. 60 (2): 109–16. doi:10.1016/s0031-9422(02)00080-8. PMID   12009313.
  6. ↑ O'Maille PE, Chappell J, Noel JP (April 2006). "Biosynthetic potential of sesquiterpene synthases: alternative products of tobacco 5-epi-aristolochene synthase". Archives of Biochemistry and Biophysics. 448 (1–2): 73–82. doi:10.1016/j.abb.2005.10.028. PMC   2859294 . PMID   16375847.
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