Epi-cedrol synthase

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

(2E,6E)-farnesyl diphosphate + H₂O

\rightleftharpoons

8-epi-cedrol + diphosphate

This enzyme is activated by Mg²⁺.

References

↑ Mercke, P., Crock, J., Croteau, R. and Brodelius, P.E. (1999). "Cloning, expression, and characterization of epi-cedrol synthase, a sesquiterpene cyclase from Artemisia annua L". Arch. Biochem. Biophys. 369: 213–222. doi:10.1006/abbi.1999.1358. PMID 10486140.
↑ Hua, L. and Matsuda, S.P. (1999). "The molecular cloning of 8-epicedrol synthase from Artemisia annua". Arch. Biochem. Biophys. 369: 208–212. doi:10.1006/abbi.1999.1357. PMID 10486139.

External links

Epi-cedrol 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)

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.