Site-directed Mutagenesis Switching a Dimethylallyl Tryptophan Synthase to a Specific Tyrosine C3-Prenylating Enzyme

• Published in: The Journal of biological chemistry Vol. 290; no. 3; pp. 1364 - 1373
• Main Authors: Fan, Aili, Zocher, Georg, Stec, Edyta, Stehle, Thilo, Li, Shu-Ming
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 16.01.2015; American Society for Biochemistry and Molecular Biology
• Subjects: Alkyl and Aryl Transferases - chemistry; Alkylation; Aspergillus; Aspergillus fumigatus - enzymology; Catalysis; Chromatography, High Pressure Liquid; Dimethylallyl Tryptophan Synthase; Enzyme Catalysis; Enzyme Mutation; Enzymology; Fungal Proteins - chemistry; Hemiterpenes - chemistry; In Vitro Mutagenesis; Indoles - chemistry; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Natural Product Biosynthesis; Organophosphorus Compounds - chemistry; Plasmids - metabolism; Prenylation; Protein Engineering; Protein Engineering - methods; Tryptophan - chemistry; Tryptophan Synthase - chemistry; Tyrosine - chemistry; Tyrosine C3-Prenyltransferase; Natural Product Biosynthesis; Aspergillus; Tyrosine C3-Prenyltransferase; Enzyme Catalysis; Protein Engineering; Dimethylallyl Tryptophan Synthase; Enzyme Mutation; Alkylation; In Vitro Mutagenesis

The tryptophan prenyltransferases FgaPT2 and 7-DMATS (7-dimethylallyl tryptophan synthase) from Aspergillus fumigatus catalyze C4- and C7-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 accep...