ArticleAngewandte Chemie (International ed. in English)2023
Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.
Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Mutasynthesis and Antibiotic Activity of Mupirocin Analogues.Chembiochem : a European journal of chemical biology · 2026Article
- An Integrated Module Performs Selective 'Online' Epoxidation in the Biosynthesis of the Antibiotic Mupirocin.Angewandte Chemie (International ed. in English) · 2024Article
- Giant polyketide synthase enzymes in the biosynthesis of giant marine polyether toxins.Science (New York, N.Y.) · 2024Article
- Giant polyketide synthase enzymes biosynthesize a giant marine polyether biotoxin.bioRxiv : the preprint server for biology · 2024Article
- Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (International ed. in English) · 2023Article
- Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Mupirocin is a clinically important antibiotic produced by a trans-AT Type I polyketide synthase (PKS) in Pseudomonas fluorescens. The major bioactive metabolite, pseudomonic acid A (PA-A), is assembled on a tetrasubstituted tetrahydropyran (THP) core incorporating a 6-hydroxy group proposed to be introduced by α-hydroxylation of the thioester of the acyl carrier protein (ACP) bound polyketide chain. Herein, we describe an in vitro approach combining purified enzyme components, chemical synthesis, isotopic labelling, mass spectrometry and NMR in conjunction with in vivo studies leading to the first characterisation of the α-hydroxylation bimodule of the mupirocin biosynthetic pathway. These studies reveal the precise timing of hydroxylation by MupA, substrate specificity and the ACP dependency of the enzyme components that comprise this α-hydroxylation bimodule. Furthermore, using purified enzyme, it is shown that the MmpA KS
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