ArticleApplied and environmental microbiology2010
Selectivity of fungal sesquiterpene synthases: role of the active site's H-1 alpha loop in catalysis.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 66 citations in OpenAlex.
- Introducing Small Rings into Farnesyl Pyrophosphates Paves the Way for the Enzymatic Generation of Unnatural Sesquiterpene Scaffolds.Journal of the American Chemical Society · 2026Article
- Molecular insights into Valencene synthase (SgTPS-V) and its role in sesquiterpenoid biosynthesis.BMC plant biology · 2026Article
- Chemoenzymatic Synthesis of Structurally Diverse Terpenoids from Farnesyl Pyrophosphates Modified at the Central Alkene Unit.Journal of the American Chemical Society · 2026Article
- Engineering Sanghuangporus sanghuang for enhanced (-)-aristolone production via metabolic pathway optimization and terpene synthase engineering.Applied microbiology and biotechnology · 2025Article
- Loop engineering of enzymes to control their immobilization and ultimately fabricate more efficient heterogeneous biocatalysts.Protein science : a publication of the Protein Society · 2025Article
- Chemoenzymatic Formation of Oxa-Terpenoids by Sesqui- and Diterpene Synthase-Mediated Biotransformations with 9-Oxy-FPP Ether Derivatives.Biochemistry · 2025Article
- Fine-Tuning the Function of Farnesene Synthases for Selective Synthesis of Farnesene Stereoisomers.Journal of agricultural and food chemistry · 2024Article
- Chromosome-Scale Genome and Transcriptomic Analyses Reveal Differential Regulation of Terpenoid Secondary Metabolites inJournal of fungi (Basel, Switzerland) · 2024Article
- Impact ofJournal of fungi (Basel, Switzerland) · 2024Article
- Unravelling the Function of the Sesquiterpene Cyclase STC3 in the Lifecycle ofInternational journal of molecular sciences · 2024Article
- Active Site Loop Engineering Abolishes Water Capture in Hydroxylating Sesquiterpene Synthases.ACS catalysis · 2023Article
- Molecular and Functional Analyses of Characterized Sesquiterpene Synthases in Mushroom-Forming Fungi.Journal of fungi (Basel, Switzerland) · 2023Article
- Biosynthesis of Sesquiterpenes in Basidiomycetes: A Review.Journal of fungi (Basel, Switzerland) · 2022Review
- Biotechnological potential and initial characterization of two novel sesquiterpene synthases from Basidiomycota Coniophora puteana for heterologous production of δ-cadinol.Microbial cell factories · 2022Article
- New Trends and Future Opportunities in the Enzymatic Formation of C-C, C-N, and C-O bonds.Chembiochem : a European journal of chemical biology · 2022Review
- A Sesquiterpene Synthase from the Endophytic FungusBiomolecules · 2021Article
- Genome sequencing of Rigidoporus microporus provides insights on genes important for wood decay, latex tolerance and interspecific fungal interactions.Scientific reports · 2020Article
- Article
- The Biogenetic Origin of the Biologically Active Naematolin of Hypholoma Species Involves an Unusual Sesquiterpene Synthase.Molecular biotechnology · 2019Article
- RNA-Seq de Novo Assembly and Differential Transcriptome Analysis of Chaga (International journal of molecular sciences · 2019Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Sesquiterpene synthases are responsible for the cyclization of farnesyl pyrophosphate into a myriad of structurally diverse compounds with various biological activities. We examine here the role of the conserved active site H-α1 loop in catalysis in three previously characterized fungal sesquiterpene synthases. The H-α1 loops of Cop3, Cop4, and Cop6 from Coprinus cinereus were altered by site-directed mutagenesis and the resultant product profiles were analyzed by gas chromatography-mass spectrometry and compared to the wild-type enzymes. In addition, we examine the effect of swapping the H-α1 loop from the promiscuous enzyme Cop4 with the more selective Cop6 and the effect of acidic or basic conditions on loop mutations in Cop4. Directed mutations of the H-α1 loop had a marked effect on the product profile of Cop3 and Cop4, while little to no change was shown in Cop6. Swapping of the Cop4 and Cop6 loops with one another was again shown to influence the product profile of Cop4, while the product profile of Cop6 remained identical to the wild-type enzyme. The loop mutations in Cop4 also implicate specific residues responsible for the pH sensitivity of the enzyme. These results affirm the role of the H-α1 loop in catalysis and provide a potential target to increase the product diversity of terpene synthases.
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