ArticleAngewandte Chemie (International ed. in English)2016
Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Genetically engineered Streptomyces viridosporus ATCC 14672 strains for the discovery of novel moenomycins.Scientific reports · 2026Article
- Article
- Structural diversity, bioactivity, and biosynthesis of phosphoglycolipid family antibiotics: Recent advances.BBA advances · 2022Article
- Bacterial terpenome.Natural product reports · 2021Review
- Bacterial diterpene synthases prenylate small molecules.ACS catalysis · 2021Article
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- Structure, Dynamics and Cellular Insight Into Novel Substrates of theFrontiers in molecular biosciences · 2020Article
- Crystal structure of TchmY from Actinoplanes teichomyceticus.Acta crystallographica. Section F, Structural biology communications · 2019Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 4 countries.
Funding
Abstract
The structure of MoeN5, a unique prenyltransferase involved in the biosynthesis of the antibiotic moenomycin, is reported. MoeN5 catalyzes the reaction of geranyl diphosphate (GPP) with the cis-farnesyl group in phosphoglycolipid 5 to form the (C25) moenocinyl-sidechain-containing lipid 7. GPP binds to an allylic site (S1) and aligns well with known S1 inhibitors. Alkyl glycosides, glycolipids, can bind to both S1 and a second site, S2. Long sidechains in S2 are "bent" and co-locate with the homoallylic substrate isopentenyl diphosphate in other prenyltransferases. These observations support a MoeN5 mechanism in which 5 binds to S2 with its C6-C11 group poised to attack C1 in GPP to form the moenocinyl sidechain, with the more distal regions of 5 aligning with the distal glucose in decyl maltoside. The results are of general interest because they provide the first structures of MoeN5 and a structural basis for its mechanism of action, results that will facilitate the design of new antibiotics.
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