ArticleJournal of the American Chemical Society2011
Two distinct mechanisms for TIM barrel prenyltransferases in bacteria.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- LipoproteinmBio · 2025Article
- Structural diversity, bioactivity, and biosynthesis of phosphoglycolipid family antibiotics: Recent advances.BBA advances · 2022Article
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- Terretonin N: A New Meroterpenoid from Nocardiopsis sp.Molecules (Basel, Switzerland) · 2018Article
- Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes in Bacillus subtilis.The Journal of biological chemistry · 2016Article
- Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.Angewandte Chemie (International ed. in English) · 2016Article
- Article
- MoeH5: a natural glycorandomizer from the moenomycin biosynthetic pathway.Molecular microbiology · 2013Article
- Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus.Chembiochem : a European journal of chemical biology · 2013Article
- Insights into the mechanism of the antibiotic-synthesizing enzyme MoeO5 from crystal structures of different complexes.Angewandte Chemie (International ed. in English) · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The reactions of two bacterial TIM barrel prenyltransferases (PTs), MoeO5 and PcrB, were explored. MoeO5, the enzyme responsible for the first step in moenomycin biosynthesis, catalyzes the transfer of farnesyl to 3-phosphoglyceric acid (3PG) to give a product containing a cis-allylic double bond. We show that this reaction involves isomerization to a nerolidyl pyrophosphate intermediate followed by bond rotation prior to attack by the nucleophile. This mechanism is unprecedented for a prenyltransferase that catalyzes an intermolecular coupling. We also show that PcrB transfers geranyl and geranylgeranyl groups to glycerol-1-phosphate (G1P), making it the first known bacterial enzyme to use G1P as a substrate. Unlike MoeO5, PcrB catalyzes prenyl transfer without isomerization to give products that retain the trans-allylic bond of the prenyl donors. The TIM barrel family of PTs is unique in including enzymes that catalyze prenyl transfer by distinctly different reaction mechanisms.
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