Discover Community Create You

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

Multienzyme docking in hybrid megasynthetases.

Nature chemical biology - 1 Jan 2008

Richter Carsten D, Nietlispach Daniel, Broadhurst R William, Weissman Kira J

Abstract excerpt

Hybrid multienzyme systems composed of polyketide synthase (PKS) and nonribosomal polypeptide synthetase (NRPS) modules direct the biosynthesis of clinically valuable natural products in bacteria. The fidelity of this process depends on specific recognition between successive polypeptides in each assembly line-interactions that are mediated by terminal 'docking domains'. We have identified a new family of...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Binding Sites
Share to Genetic Engineering

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Models, Molecular

Share to Multienzyme Complexes

Share to Peptide Synthases

Share to Polyketide Synthases

Source

Identifiers

PMID: 18066054
DOI: 10.1038/nchembio.2007.61

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multienzyme docking in hybrid megasynthetases.PMID 18066054Read ↗

Protein–Protein Interactions in Multienzyme MegasynthetasesSemantic proximity Read ↗

Identification and analysis of the core biosynthetic machinery of tubulysin, a potent cytotoxin with potential anticancer activity.Semantic proximity Read ↗

Structural basis of the interaction of MbtH-like proteins, putative regulators of nonribosomal peptide biosynthesis, with adenylating enzymes.Semantic proximity Read ↗

Harnessing the potential of communication-mediating domains for the biocombinatorial synthesis of nonribosomal peptides.Semantic proximity Read ↗

Insights into a type III cohesin-dockerin recognition interface from the cellulose-degrading bacterium Ruminococcus flavefaciens.Semantic proximity Read ↗

Prediction of inter domain interactions in modular polyketide synthases by docking and correlated mutation analysis.Semantic proximity Read ↗

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.Semantic proximity Read ↗

Linker Flexibility Facilitates Module Exchange in Fungal Hybrid PKS-NRPS EngineeringSemantic proximity Read ↗

Biosynthesis of the dideoxysugar component of jadomycin B: genes in the jad cluster of Streptomyces venezuelae ISP5230 for L-digitoxose assembly and transfer to the angucycline aglycone.Semantic proximity Read ↗

Domain-domain interactions in the iterative type I polyketide synthase ATX from Aspergillus terreus.Semantic proximity Read ↗

Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains.Semantic proximity Read ↗

Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway.Semantic proximity Read ↗

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