ArticleFrontiers in plant science2012
Benzalacetone synthase.
Article in Frontiers in plant science, 2012. 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, 13 citations in OpenAlex.
- Optimizing MatB-MatC-Dependent Malonyl-CoA Supply for Enhanced Raspberry Ketone Production inBiotech (Basel (Switzerland)) · 2026Article
- Single-cell RNA-sequencing of Nicotiana attenuata corolla cells reveals the biosynthetic pathway of a floral scent.The New phytologist · 2022Article
- Engineered biosynthesis of plant polyketides by type III polyketide synthases in microorganisms.Frontiers in bioengineering and biotechnology · 2022Review
- Engineering intracellular malonyl-CoA availability in microbial hosts and its impact on polyketide and fatty acid synthesis.Applied microbiology and biotechnology · 2020Review
- Synthesis of the character impact compound raspberry ketone and additional flavoring phenylbutanoids of biotechnological interest with Corynebacterium glutamicum.Microbial cell factories · 2020Article
- Engineering microbes for plant polyketide biosynthesis.Computational and structural biotechnology journal · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Benzalacetone synthase, from the medicinal plant Rheum palmatum (RpBAS), is a plant-specific chalcone synthase (CHS) superfamily of type III polyketide synthase (PKS). RpBAS catalyzes the one-step, decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the C(6)-C(4) benzalacetone scaffold. The X-ray crystal structures of RpBAS confirmed that the diketide-forming activity is attributable to the characteristic substitution of the conserved active-site "gatekeeper" Phe with Leu. Furthermore, the crystal structures suggested that RpBAS employs novel catalytic machinery for the thioester bond cleavage of the enzyme-bound diketide intermediate and the final decarboxylation reaction to produce benzalacetone. Finally, by exploiting the remarkable substrate tolerance and catalytic versatility of RpBAS, precursor-directed biosynthesis efficiently generated chemically and structurally divergent, unnatural novel polyketide scaffolds. These findings provided a structural basis for the functional diversity of the type III PKS enzymes.
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Registered trials
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