Elisabethatriene synthase

Identifiers

Databases

PDB structures

Elisabethatriene synthase (EC 4.2.3.41, elisabethatriene cyclase) is an enzyme with systematic name geranylgeranyl-diphosphate diphosphate-lyase (elisabethatriene-forming).^[1]^[2] This enzyme catalyses the following chemical reaction

\rightleftharpoons

elisabethatriene + diphosphate

This enzyme requires Mg²⁺ or less efficiently Mn²⁺.

References

↑ Kohl, A.C.; Kerr, R.G. (2004). "Identification and characterization of the pseudopterosin diterpene cyclase, elisabethatriene synthase, from the marine gorgonian, Pseudopterogorgia elisabethae". Arch. Biochem. Biophys. 424: 97–104. doi:10.1016/j.abb.2004.01.019. PMID 15019841.
↑ Bruck, T.B.; Kerr, R.G. (2006). "Purification and kinetic properties of elisabethatriene synthase from the coral Pseudopterogorgia elisabethae". Comp. Biochem. Physiol. B Biochem. Mol. Biol. 143: 269–278. doi:10.1016/j.cbpb.2005.11.016. PMID 16423548.

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 5/18/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.