ArticleAngewandte Chemie (International ed. in English)2021
Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme.
Article in Angewandte Chemie (International ed. in English), 2021. 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, 17 citations in OpenAlex.
- Orsellinic Acid from the EndophyticACS omega · 2026Article
- A hybrid assembly mechanism employs nonreducing polyketide synthase-like logic for partially reduced polyketide formation.Marine life science & technology · 2026Article
- Metabolic Blockade-Based Genome Mining ofMarine drugs · 2025Article
- The terrein biosynthetic gene cluster ofFrontiers in fungal biology · 2025Review
- Combinatorial biosynthesis for the engineering of novel fungal natural products.Communications chemistry · 2024Review
- Genomics-driven derivatization of the bioactive fungal sesterterpenoid variecolin: Creation of an unnatural analogue with improved anticancer properties.Acta pharmaceutica Sinica. B · 2024Article
- Activation of a Silent Polyketide Synthase SlPKS4 Encoding the CMarine drugs · 2023Article
- Basidiomycete non-reducing polyketide synthases function independently of SAT domains.Fungal biology and biotechnology · 2023Article
- EngineeringJournal of fungi (Basel, Switzerland) · 2021Article
- Early Oxidative Transformations During the Biosynthesis of Terrein and Related Natural Products.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme.Angewandte Chemie (International ed. in English) · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polyketide synthase (PKS)-like protein TerB, consisting of inactive dehydratase, inactive C-methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6-hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans-interaction between iterative PKS components.
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Registered trials
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