Alpha-muurolene synthase

Alpha-muurolene synthase (EC 4.2.3.125, Cop3) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, alpha-muurolene-forming).^[1]^[2] This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate

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alpha-muurolene + diphosphate

The enzyme has been characterized from the fungus Coprinus cinereus.

References

↑ Agger, S.; Lopez-Gallego, F.; Schmidt-Dannert, C. (2009). "Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus". Mol. Microbiol. 72: 1181–1195. doi:10.1111/j.1365-2958.2009.06717.x. PMID 19400802.
↑ Lopez-Gallego, F.; Wawrzyn, G.T.; Schmidt-Dannert, C. (2010). "Selectivity of fungal sesquiterpene synthases: role of the active site’s H-1α loop in catalysis". Appl. Environ. Microbiol. 76: 7723–7733. doi:10.1128/aem.01811-10. PMID 20889795.

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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