ArticleNature chemical biology2020
The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Metabologenomic Hallmark-Based Discovery of Bacterial Thioamides as a New Lead against Drug-Resistant Pancreatic Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- An α/β-Hydrolase GmABHD6 Controls Seed Oil Content and Yield in Soybean.Plant biotechnology journal · 2026Article
- Epimerisation in Peptide Synthesis.Molecules (Basel, Switzerland) · 2023Review
- Electrochemical carbon-carbon coupling with enhanced activity and racemate stereoselectivity by microenvironment regulation.Nature communications · 2023Article
- Cytochromes P450 Associated with the Biosyntheses of Ribosomally Synthesized and Post-translationally Modified Peptides.ACS bio & med chem Au · 2023Review
- Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism.Nature communications · 2023Article
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Thiamyxins: Structure and Biosynthesis of Myxobacterial RNA-Virus Inhibitors.Angewandte Chemie (International ed. in English) · 2022Article
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- Methionine epimerization in cyclic peptides.RSC advances · 2021Article
- Identification of the peptide epimerase MslH responsible for d-amino acid introduction at the C-terminus of ribosomal peptides.Chemical science · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
D-amino acids endow peptides with diverse, desirable properties, but the post-translational and site-specific epimerization of L-amino acids into their D-counterparts is rare and chemically challenging. Bottromycins are ribosomally synthesized and post-translationally modified peptides that have overcome this challenge and feature a D-aspartate (D-Asp), which was proposed to arise spontaneously during biosynthesis. We have identified the highly unusual α/β-hydrolase (ABH) fold enzyme BotH as a peptide epimerase responsible for the post-translational epimerization of L-Asp to D-Asp during bottromycin biosynthesis. The biochemical characterization of BotH combined with the structures of BotH and the BotH-substrate complex allowed us to propose a mechanism for this reaction. Bioinformatic analyses of BotH homologs show that similar ABH enzymes are found in diverse biosynthetic gene clusters. This places BotH as the founding member of a group of atypical ABH enzymes that may be able to epimerize non-Asp stereocenters across different families of secondary metabolites.
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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.