The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Crystal Structure of Pentalenene Synthase: Mechanistic Insights on Terpenoid Cyclization Reactions in Biology
Abstract
The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the α-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.
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Cited by
Metal ions in biological catalysis: from enzyme databases to general principles
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Plant terpenoid synthases: Molecular biology and phylogenetic analysis
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Bacterial volatiles: the smell of small organisms
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Structural Biology and Chemistry of the Terpenoid Cyclases
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Metadata
- Authors
- Lesburg, C. A., Zhai, G., Cane, D. E., & Christianson, D. W.
- Venue
- Science
- Published
- 1997-09-19
- Volume
- 277
- Issue
- 5333
- Pages
- 1820-1824
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2056400844
- Cited by
- 454
- References
- 29
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lesburg, C. A., Zhai, G., Cane, D. E., & Christianson, D. W. (1997). Crystal Structure of Pentalenene Synthase: Mechanistic Insights on Terpenoid Cyclization Reactions in Biology. Science. https://doi.org/10.1126/science.277.5333.1820
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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