Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insights into azalomycin F assembly-line contribute to evolution-guided polyketide synthase engineering and identification of intermodular recognition

4 Feb 2023

Abstract excerpt

Abstract Modular polyketide synthase (PKS) is an ingenious core machine that catalyzes abundant polyketides in nature. Exploring interactions among modules in PKS is very important for understanding the overall biosynthetic process and for engineering PKS assembly-lines. Here, we show that intermodular recognition between the enoylreductase domain ER1/2 inside module 1/2 and the ketosynthase domain KS3 inside...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Genomics and Phylogenetic Studies
Share to Microbial Natural Products and Biosynthesis
Share to Plant Disease Resistance and Genetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36739290
DOI: 10.1038/s41467-023-36213-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into azalomycin F assembly-line contribute to evolution-guided polyketide synthase engineering and identification of intermodular recognitionPMID 36739290Read ↗

An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain.Semantic proximity Read ↗

The modules of trans-acyltransferase assembly lines redefined with a central acyl carrier protein.Semantic proximity Read ↗

Ketosynthase Domain Constrains the Design of Polyketide Synthases.Semantic proximity Read ↗

Structural rearrangements of a polyketide synthase module during its catalytic cycleSemantic proximity Read ↗

Roles of Conserved Active Site Residues in the Ketosynthase Domain of an Assembly Line Polyketide Synthase.Semantic proximity Read ↗

Combinatorialization of fungal polyketide synthase-peptide synthetase hybrid proteins.Semantic proximity Read ↗

Characterization of Giant Modular PKSs Provides Insight into Genetic Mechanism for Structural Diversification of Aminopolyol PolyketidesSemantic proximity Read ↗

Emulating evolutionary processes to morph aureothin-type modular polyketide synthases and associated oxygenasesSemantic proximity Read ↗

Diversity oriented biosynthesis via accelerated evolution of modular gene clusters.Semantic proximity Read ↗

Structural Insight into the Reaction Mechanism of Ketosynthase-Like Decarboxylase in a Loading Module of Modular Polyketide Synthases.Semantic proximity Read ↗

Coevolution-based prediction of protein-protein interactions in polyketide biosynthetic assembly linesSemantic proximity Read ↗

Unraveling the iterative type I polyketide synthases hidden in StreptomycesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.