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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.

SUBMITTER: Hyatt DC

PROVIDER: S-EPMC1838495 | biostudies-other | 2007 Mar

REPOSITORIES: biostudies-other

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Structure of limonene synthase, a simple model for terpenoid cyclase catalysis.

Hyatt David C DC Youn Buhyun B Zhao Yuxin Y Santhamma Bindu B Coates Robert M RM Croteau Rodney B RB Kang ChulHee C

Proceedings of the National Academy of Sciences of the United States of America 20070319 13

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 coo ...[more]

PMID: 17372193

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