title: Structure of limonene synthase, a simple model for terpenoid cyclase catalysis.
abstract: The crystal structure of (4S)-limonene synthase from Mentha spic ata, a metal ion-dependent monoterpene cyclase that catalyzes the coupled isomerization and cyclization of geranyl diphosphate, is reported at 2.7-A; resolution in two forms liganded to the substrate and intermediate analogs, 2-fluorogeranyl diphosphate and 2-fluorolinalyl diphosphate, respectively. The implications of these findings are described for domain interactions in the homodimer and for changes in diphosphate-metal ion coordination and substrate binding conformation in the course of the multistep reaction.
authors: Institute of Biological Chemistry, Washingston State University, Pullman, WA 99164-6340, USA.
authors: David C
authors: DC
authors: Hyatt
authors: Buhyun
authors: B
authors: Youn
authors: Yuxin
authors: Y
authors: Zhao
authors: Bindu
authors: B
authors: Santhamma
authors: Robert M
authors: RM
authors: Coates
authors: Rodney B
authors: RB
authors: Croteau
authors: ChulHee
authors: C
authors: Kang
mesh_terms: D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D019753:Intramolecular Lyases / Q000737:chemistry* / Q000378:metabolism; D007477:Ions; D008024:Ligands; D031337:Mentha spicata / Q000201:enzymology; D008956:Models, Chemical; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D013729:Terpenes / Q000737:chemistry*
chemical_list: D007477:Ions; D008024:Ligands; D010940:Plant Proteins; D013729:Terpenes; D019753:Intramolecular Lyases; C040265:pinene cyclase I