ReviewBeilstein journal of organic chemistry2019
Molecular basis for the plasticity of aromatic prenyltransferases in hapalindole biosynthesis.
Review in Beilstein journal of organic chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Cyanobacteria: A Promising Source of Antifungal Metabolites.Marine drugs · 2023Review
- Structural Basis of Substrate Promiscuity and Catalysis by the Reverse PrenyltransferaseBiochemistry · 2022Article
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- Acceptor substrate determines donor specificity of an aromatic prenyltransferase: expanding the biocatalytic potential of NphB.Applied microbiology and biotechnology · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Aromatic prenyltransferases (PTases) are enzymes that catalyze Friedel-Crafts reactions between aromatic compounds and isoprenoid diphosphates. In hapalindole biosynthesis, the aromatic PTases AmbP1 and AmbP3 exhibit surprisingly plastic selectivities. AmbP1 not only transfers the geranyl group on the C-3 of
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