1,8-cineole synthase

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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).^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

geranyl diphosphate + H₂O

\rightleftharpoons

1,8-cineole + diphosphate

This enzyme requires Mn²⁺ or Zn²⁺.

References

↑ Croteau, R., Alonso, W.R., Koepp, A.E. and Johnson, M.A. (1994). "Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase". Arch. Biochem. Biophys. 309: 184–192. doi:10.1006/abbi.1994.1101. PMID 8117108.
↑ Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. (1998). "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: 14891–14899. doi:10.1074/jbc.273.24.14891. PMID 9614092.
↑ Peters, R.J. and Croteau, R.B. (2003). "Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases". Arch. Biochem. Biophys. 417: 203–211. doi:10.1016/s0003-9861(03)00347-3. PMID 12941302.
↑ Chen, F., Ro, D.K., Petri, J., Gershenzon, J., Bohlmann, J., Pichersky, E. and Tholl, D. (2004). "Characterization of a root-specific Arabidopsis terpene synthase responsible for the formation of the volatile monoterpene 1,8-cineole". Plant Physiol. 135: 1956–1966. doi:10.1104/pp.104.044388. PMID 15299125.
↑ Keszei, A., Brubaker, C.L., Carter, R., Kollner, T., Degenhardt, J. and Foley, W.J. (2010). "Functional and evolutionary relationships between terpene synthases from Australian Myrtaceae". Phytochemistry 71: 844–852. doi:10.1016/j.phytochem.2010.03.013. PMID 20399476.

External links

1,8-cineole synthase at the US National Library of Medicine Medical Subject Headings (MeSH)

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

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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