ArticleJournal of the American Chemical Society2013
Multisite prenylation of 4-substituted tryptophans by dimethylallyltryptophan synthase.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 41 citations in OpenAlex.
- Data Science-Driven Analysis of Substrate-Permissive Diketopiperazine Reverse Prenyltransferase NotF: Applications in Protein Engineering and Cascade Biocatalytic Synthesis of (-)-Eurotiumin A.Journal of the American Chemical Society · 2022Article
- Regioselective Biocatalytic C4-Prenylation of Unprotected Tryptophan Derivatives.Chembiochem : a European journal of chemical biology · 2022Article
- Biosynthesis and trafficking of hemeCritical reviews in biochemistry and molecular biology · 2021Review
- Article
- Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases.Nature communications · 2020Article
- Acceptor substrate determines donor specificity of an aromatic prenyltransferase: expanding the biocatalytic potential of NphB.Applied microbiology and biotechnology · 2020Article
- Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.Natural product reports · 2020Review
- Article
- Molecular basis for the plasticity of aromatic prenyltransferases in hapalindole biosynthesis.Beilstein journal of organic chemistry · 2019Review
- Structure and specificity of a permissive bacterial C-prenyltransferase.Nature chemical biology · 2017Article
- C7-derivatization of C3-alkylindoles including tryptophans and tryptamines.The Journal of organic chemistry · 2014Article
- δ-Deuterium isotope effects as probes for transition-state structures of isoprenoid substrates.The Journal of organic chemistry · 2014Article
- Synthesis of 2-substituted tryptophans via a C3- to C2-alkyl migration.Beilstein journal of organic chemistry · 2014Article
- Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives.ACS chemical biology · 2013Article
- Palladium-catalyzed synthesis of N-tert-prenylindoles.Organic letters · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The aromatic prenyltransferase dimethylallyltryptophan synthase in Claviceps purpurea catalyzes the normal prenylation of tryptophan at C4 of the indole nucleus in the first committed step of ergot alkaloid biosynthesis. 4-Methyltryptophan is a competitive inhibitor of the enzyme that has been used in kinetic studies. Upon investigation of background activity during incubations of 4-methyltryptophan with dimethylallyl diphosphate, we found that the analogue was an alternate substrate, which gave four products. The structures of three of these compounds were established by (1)H NMR and 2D NMR studies and revealed that dimethylallyltryptophan synthase catalyzed both normal and reverse prenylation at C3 of the indole ring and normal prenylation of N1. Similarly, 4-methoxytryptophan was an alternate substrate, giving normal prenylation at C5 as the major product. 4-Aminotryptophan, another alternate substrate, gave normal prenylation at C5 and C7. The ability of dimethylallyltryptophan synthase to prenylate at five different sites on the indole nucleus, with normal and reverse prenylation at one of the sites, is consistent with a dissociative electrophilic alkylation of the indole ring, where orientation of the substrates within the active site and substituent electronic effects determine the position and type of prenylation. These results suggest a common mechanism for prenylation of tryptophan by all of the members of the structurally related dimethylallyltryptophan synthase family.
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