Journal article
Structure of limonene synthase, a simple model for terpenoid cyclase catalysis
Proceedings of the National Academy of Sciences - PNAS, Vol.104(13), pp.5360-5365
03/27/2007
Handle:
https://hdl.handle.net/2376/112943
PMCID: PMC1838495
PMID: 17372193
Abstract
The crystal structure of (4
S
)-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-Å; 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.
Metrics
12 Record Views
Details
- Title
- Structure of limonene synthase, a simple model for terpenoid cyclase catalysis
- Creators
- David C Hyatt - Institute of Biological Chemistry, Washingston State University, Pullman, WA 99164-6340Buhyun Youn - School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4660; andYuxin Zhao - Department of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801Bindu Santhamma - Department of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801Robert M Coates - Department of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801Rodney B Croteau - Institute of Biological Chemistry, Washingston State University, Pullman, WA 99164-6340ChulHee Kang - School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4660; and
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.104(13), pp.5360-5365
- Academic Unit
- Chemistry, Department of; Biological Chemistry, Institute of
- Publisher
- National Academy of Sciences
- Identifiers
- 99900547789001842
- Language
- English
- Resource Type
- Journal article