(+)-alpha-santalene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing)

(+)-alpha-santalene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing) (EC 4.2.3.50, SBS) is an enzyme with systematic name (2Z,6Z)-farnesyl diphosphate lyase (cyclizing; (+)-alpha-santalene-forming).^[1] This enzyme catalyses the following chemical reaction

(2Z,6Z)-farnesyl diphosphate

\rightleftharpoons

(+)-alpha-santalene + diphosphate

The enzyme synthesizes a mixture of sesquiterpenoids from (2Z,6Z)-farnesyl diphosphate.

References

↑ Sallaud, C., Rontein, D., Onillon, S., Jabes, F., Duffe, P., Giacalone, C., Thoraval, S., Escoffier, C., Herbette, G., Leonhardt, N., Causse, M. and Tissier, A. (2009). "A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites". Plant Cell 21: 301–317. doi:10.1105/tpc.107.057885. PMID 19155349.

External links

( )-alpha-santalene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing) 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.