ArticleThe Journal of biological chemistry2015
Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Elucidation of the Verrucofortine Biosynthetic Pathway Enables Identification of a Cyclodipeptide Prenyltransferase with High Catalytic Efficiency.Journal of agricultural and food chemistry · 2026Article
- Substrate-Multiplexed Assessment of Aromatic Prenyltransferase Activity.Chembiochem : a European journal of chemical biology · 2025Article
- Discovery and Heterologous Expression of Functional 4-Journal of natural products · 2024Article
- Structure-guided Mutagenesis Reveals the Catalytic Residue that Controls the Regiospecificity of C6-Indole Prenyltransferases.ChemCatChem · 2023Article
- Biocatalytic Friedel-Crafts Reactions.ChemCatChem · 2022Review
- Synthetic production of prenylated naringenins in yeast using promiscuous microbial prenyltransferases.Metabolic engineering communications · 2021Article
- Recent advances in biocatalytic derivatization of L-tyrosine.Applied microbiology and biotechnology · 2020Review
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- Enzymatic studies on aromatic prenyltransferases.Journal of natural medicines · 2020Review
- Vib-PT, an Aromatic Prenyltransferase Involved in the Biosynthesis of Vibralactone fromApplied and environmental microbiology · 2020Article
- Acceptor substrate determines donor specificity of an aromatic prenyltransferase: expanding the biocatalytic potential of NphB.Applied microbiology and biotechnology · 2020Article
- Building Bridges: Biocatalytic C-C-Bond Formation toward Multifunctional Products.ACS catalysis · 2016Review
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
The tryptophan prenyltransferases FgaPT2 and 7-DMATS (7-dimethylallyl tryptophan synthase) from Aspergillus fumigatus catalyze C(4)- and C(7)-prenylation of the indole ring, respectively. 7-DMATS was found to accept l-tyrosine as substrate as well and converted it to an O-prenylated derivative. An acceptance of l-tyrosine by FgaPT2 was also observed in this study. Interestingly, isolation and structure elucidation revealed the identification of a C(3)-prenylated l-tyrosine as enzyme product. Molecular modeling and site-directed mutagenesis led to creation of a mutant FgaPT2_K174F, which showed much higher specificity toward l-tyrosine than l-tryptophan. Its catalytic efficiency toward l-tyrosine was found to be 4.9-fold in comparison with that of non-mutated FgaPT2, whereas the activity toward l-tryptophan was less than 0.4% of that of the wild-type. To the best of our knowledge, this is the first report on an enzymatic C-prenylation of l-tyrosine as free amino acid and altering the substrate preference of a prenyltransferase by mutagenesis.
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