Aristolochene synthase

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming). Other names in common use include sesquiterpene cyclase, trans,trans-farnesyl diphosphate aristolochene-lyase, trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,, and aristolochene-forming). This enzyme participates in terpenoid biosynthesis.

This protein may use the morpheein model of allosteric regulation. ^[1]

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2E4O and 2OA6. They are both notable for the very high helix content of the structure.

References

↑ T. Selwood and E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

Cane DE, Prabhakaran PC, Oliver JS and McIlwaine DB (1990). "Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate". J. Am. Chem. Soc. 112 (8): 3209–3210. doi:10.1021/ja00164a051.
Noguchi H and Rawlings BJ (1989). "Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate". J. Am. Chem. Soc. 111 (24): 8914–8916. doi:10.1021/ja00206a022.
Hohn TM, Plattner RD (1989). "Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti". Arch. Biochem. Biophys. 272 (1): 137–43. doi:10.1016/0003-9861(89)90204-X. PMID 2544140.
Proctor RH, Hohn TM (1993). "Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti". J. Biol. Chem. 268 (6): 4543–8. PMID 8440737.
Calvert MJ, Ashton PR, Allemann RK (2002). "Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene". J. Am. Chem. Soc. 124 (39): 11636–41. doi:10.1021/ja020762p. PMID 12296728.

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

Proteins: 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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