5-epiaristolochene synthase

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). This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate

\rightleftharpoons

(+)-5-epiaristolochene + diphosphate

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

References

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.
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.
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.
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.
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.
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.

External links

5-epiaristolochene+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 4.2.3