ReviewApplied microbiology and biotechnology2014
Roles of type II thioesterases and their application for secondary metabolite yield improvement.
Review in Applied microbiology and biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 95 citations in OpenAlex.
- Reprogramming the enduracidin NRPS assembly line via thioesterase domain relocation.Synthetic and systems biotechnology · 2027Article
- Sustainable Biocatalytic Cascades: A Versatile Tool in the Synthesis of Natural Products With Therapeutic Potential.Chembiochem : a European journal of chemical biology · 2026Review
- Activation of a gene cluster in Streptomyces lavendulae subsp. lavendulae CCM 3239 induced strevertene production.Applied microbiology and biotechnology · 2026Article
- Genetic modifications boost chrexanthomycin yield and neuroprotective potential.Journal of advanced research · 2026Article
- Polyketide synthase-based controlled synthesis of polycyclopropanated fuel molecules.Nature communications · 2026Article
- Modular biosynthesis of microbiome-derived polyketides and nonribosomal peptides: insights and opportunities for Lactobacillaceae.Microbial cell factories · 2026Review
- A single lysergyl peptide synthetase assembles lysergic acid amides in Aspergillus species.PloS one · 2026Article
- Computational mass spectrometry and genome mining guided discovery of metallophores produced by Microbulbifer.ISME communications · 2026Article
- Non-canonical thioesterases in bacterial non-ribosomal peptide biosynthesis.The Journal of antibiotics · 2025Review
- EngineeringACS sustainable chemistry & engineering · 2025Article
- Fatuamide A, a Hybrid PKS/NRPS Metallophore from aJournal of natural products · 2025Article
- Article
- Refactoring the pikromycin synthase for the modular biosynthesis of macrolide antibiotics in E. coli.Research square · 2025Article
- Gene editing of the thioester reductase step in the biosynthesis of lysergic acid amides.PloS one · 2025Article
- Engineering thioesterase as a driving force for novel itaconate production via its degradation scheme.Metabolic engineering communications · 2024Article
- Combinatorial metabolic engineering of Streptomyces sp. CB03234-S for the enhanced production of anthraquinone-fused enediyne tiancimycins.Microbial cell factories · 2024Article
- Unveiling a CAAX Protease-Like Protein Involved in Didemnin Drug Maturation and Secretion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Crosstalk between primary and secondary metabolism: Interconnected fatty acid and polyketide biosynthesis in prokaryotes.Bioorganic & medicinal chemistry letters · 2023Review
- Unique Initiation and Termination Mechanisms Involved in the Biosynthesis of a Hybrid Polyketide-Nonribosomal Peptide Lyngbyapeptin B Produced by the Marine CyanobacteriumACS chemical biology · 2023Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A large number of antibiotics and other industrially important microbial secondary metabolites are synthesized by polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs). These multienzymatic complexes provide an enormous flexibility in formation of diverse chemical structures from simple substrates, such as carboxylic acids and amino acids. Modular PKSs and NRPSs, often referred to as megasynthases, have brought about a special interest due to the colinearity between enzymatic domains in the proteins working as an "assembly line" and the chain elongation and modification steps. Extensive efforts toward modified compound biosynthesis by changing organization of PKS and NRPS domains in a combinatorial manner laid good grounds for rational design of new structures and their controllable biosynthesis as proposed by the synthetic biology approach. Despite undeniable progress made in this field, the yield of such "unnatural" natural products is often not satisfactory. Here, we focus on type II thioesterases (TEIIs)--discrete hydrolytic enzymes often encoded within PKS and NRPS gene clusters which can be used to enhance product yield. We review diverse roles of TEIIs (removal of aberrant residues blocking the megasynthase, participation in substrate selection, intermediate, and product release) and discuss their application in new biosynthetic systems utilizing PKS and NRPS parts.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.