ArticleProceedings of the National Academy of Sciences of the United States of America2006
Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
86 citing papers in PubMed, 220 citations in OpenAlex.
- Reprogramming product selectivity and activity in promiscuous terpene synthases via substrate conformation engineering.Nature communications · 2026Article
- Designed Water Capture in Terpene Synthase Catalysis.Chembiochem : a European journal of chemical biology · 2026Article
- A multifunctional sesquiterpene synthase integrates with cytochrome P450s to reinforce the terpenoid defense network in maize.The Plant journal : for cell and molecular biology · 2025Article
- Rapid Screening of Plastic-Degrading Enzymes Using an Optimized Cell-Free Protein Synthesis Platform.Journal of microbiology and biotechnology · 2025Article
- Systematic biotechnological production of isoprenoid analogs with bespoke carbon skeletons.Nature communications · 2025Article
- Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues.Chemical communications (Cambridge, England) · 2025Review
- Simulation-Guided Engineering Enables a Functional Switch in Selinadiene Synthase toward Hydroxylation.ACS catalysis · 2024Article
- Carotenoid cleavage enzymes evolved convergently to generate the visual chromophore.Nature chemical biology · 2024Article
- Differential Substrate Sensing in Terpene Synthases from Plants and Microorganisms: Insight from Structural, Bioinformatic, and EnzyDock Analyses.Angewandte Chemie (International ed. in English) · 2024Article
- A century of studying plant secondary metabolism-From "what?" to "where, how, and why?"Plant physiology · 2024Review
- Cyclization mechanism of monoterpenes catalyzed by monoterpene synthases in dipterocarpaceae.Synthetic and systems biotechnology · 2024Article
- Coevolutionary Information Captures Catalytic Functions and Reveals Divergent Roles of Terpene Synthase Interdomain Connections.Biochemistry · 2024Article
- Overexpression of theFrontiers in plant science · 2024Article
- Mechanistic docking in terpene synthases using EnzyDock.Methods in enzymology · 2024Review
- Active Site Loop Engineering Abolishes Water Capture in Hydroxylating Sesquiterpene Synthases.ACS catalysis · 2023Article
- Expanding the terpene biosynthetic code with non-canonical 16 carbon atom building blocks.Nature communications · 2022Article
- Predictive Engineering of Class I Terpene Synthases Using Experimental and Computational Approaches.Chembiochem : a European journal of chemical biology · 2022Review
- Evolution of DIMBOA-GlcMolecules (Basel, Switzerland) · 2022Article
- Engineering of Ancestors as a Tool to Elucidate Structure, Mechanism, and Specificity of Extant Terpene Cyclase.Journal of the American Chemical Society · 2021Article
- Integrating structure-based machine learning and co-evolution to investigate specificity in plant sesquiterpene synthases.PLoS computational biology · 2021Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Terpene synthases are a mechanistically intriguing family of enzymes that catalyze complex, multistep reactions that are capable of generating hundreds of structurally diverse hydrocarbon and oxygenated scaffolds of biological and commercial importance. Interestingly, distantly related terpene synthases from fungi to plants all contain an invariant three-dimensional fold, and molecular comparisons of their active sites indicate that they are enriched with relatively inert amino acid residues that do not react directly with the reaction intermediates. Therefore, catalytic specificity appears to rely on the contour and dynamics of the active site created by the positioning of amino acid backbones and side chains on this catalytic surface and by supporting layers of residues surrounding the synthase active site cavity. Despite the high degree of structural relatedness among terpene synthases, previous studies suggest that no clear relationship between phylogenic organization and catalytic specificities is easily deciphered. We now report on the reciprocal interconversion of catalytic specificities between two distinct yet evolutionarily related terpene synthases based on the systematic identification and mutational replacement of variable residues within and surrounding the active site. Furthermore, we uncover previously undocumented biosynthetic activity during the interconversion, activity that could have been present in a common ancestor of these two highly related synthases. These results provide a simplified means for mapping structural features that are responsible for functional attributes and a strategy for identifying residues that differentiate divergent biosynthetic properties in phylogenetically related terpene synthases.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.