ArticleThe Journal of antibiotics2016
Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants.
Article in The Journal of antibiotics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Sequence-guided engineering of a bacterial diterpene synthase induces further cyclization.ACS catalysis · 2026Article
- Divergent Lineage of Terpene Synthases Establishes Terpenoid Biosynthesis in Brown Macroalgae.Journal of the American Chemical Society · 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
- IECata: interpretable bilinear attention network and evidential deep learning improve the catalytic efficiency prediction of enzymes.Briefings in bioinformatics · 2025Article
- Coevolutionary Information Captures Catalytic Functions and Reveals Divergent Roles of Terpene Synthase Interdomain Connections.Biochemistry · 2024Article
- Mining methods and typical structural mechanisms of terpene cyclases.Bioresources and bioprocessing · 2021Review
- Molecular and Functional Evolution of the Spermatophyte Sesquiterpene Synthases.International journal of molecular sciences · 2021Article
- Germacrene A-A Central Intermediate in Sesquiterpene Biosynthesis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Review
- Expression of the Fusarium graminearum terpenome and involvement of the endoplasmic reticulum-derived toxisome.Fungal genetics and biology : FG & B · 2019Article
- Article
- Structural and Chemical Biology of Terpenoid Cyclases.Chemical reviews · 2017Review
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plant terpene synthase (TPS) family is responsible for the biosynthesis of a variety of terpenoid natural products possessing diverse biological functions. TPSs catalyze the ionization and, most commonly, rearrangement and cyclization of prenyl diphosphate substrates, forming linear and cyclic hydrocarbons. Moreover, a single TPS often produces several minor products in addition to a dominant product. We characterized the catalytic profiles of Hyoscyamus muticus premnaspirodiene synthase (HPS) and compared it with the profile of a closely related TPS, Nicotiana tabacum 5-epi-aristolochene synthase (TEAS). The profiles of two previously studied HPS and TEAS mutants, each containing nine interconverting mutations, dubbed HPS-M9 and TEAS-M9, were also characterized. All four TPSs were compared under varying temperature and pH conditions. In addition, we solved the X-ray crystal structures of TEAS and a TEAS quadruple mutant complexed with substrate and products to gain insight into the enzymatic features modulating product formation. These informative structures, along with product profiles, provide new insight into plant TPS catalytic promiscuity.
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