Mutation on Gly115 and Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 increases its catalytic activity toward hydroxynaphthalenes

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• 作者：Wei Zhao ; Aili Fan ; Sylwia Tarcz ; Kang Zhou…
• 关键词：Hydroxynaphthalenes ; Dimethylallyltryptophan synthase ; Enzyme catalysis ; Friedel–Crafts alkylation ; Prenyltransferase
• 刊名：Applied Microbiology and Biotechnology
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：101
• 期：5
• 页码：1989-1998
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Microbiology; Microbial Genetics and Genomics; Biotechnology;
• 出版者：Springer Berlin Heidelberg
• ISSN：1432-0614
• 卷排序：101

文摘

The fungal cyclic dipeptide prenyltransferase FtmPT1 from Aspergillus fumigatus catalyzes a regular C2-prenylation of brevianamide F (cyclo-l-Trp-l-Pro) and is involved in the biosynthesis of a number of biologically active natural products including tryprostatins, spirotryprostatins, verruculogen, and fumitremorgins. FtmPT1, like other members of the dimethylallyltryptophan synthase superfamily, was shown to have high substrate promiscuity for tryptophan-containing cyclic dipeptides and a few other aromatic substrates. A previous study demonstrated the acceptance of 1-naphthol by FtmPT1, but with very low product yield. In this study, we report the significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by FtmPT1_G115A and six FtmPT1_Y205X single mutants as well as FtmPT1_G115A_Y205C. These results provided an example for creation of biocatalysts with improved catalytic activity by site-directed mutagenesis.