A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: Biochemical characterization and structural insight into the regioselective prenylation |
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| Affiliation: | 1. Department of System Chemotherapy and Molecular Sciences, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan;2. Faculty of Pharmacy, Kinki University, 3-4-1 Kowakae, Higashi-osaka 577-8502, Japan;1. Drug Metabolism and Pharmacokinetics, GlaxoSmithKline, Ware, Herts, SG12 0DP, UK;2. Biochemistry Department, Imperial College, London, SW7 2AZ, UK;3. Centre for Environmental Policy, Imperial College London, London, SW7 2AZ, UK;1. State Key Laboratory of Pharmaceutical Biotechnology, Institute of Functional Biomolecules, School of Life Sciences, Nanjing University, Nanjing 210023, China;2. State Key Laboratory of Coordination Chemistry, Jiangsu Key Laboratory of Advanced Organic Materials, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China |
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| Abstract: | A putative 7-dimethylallyl tryptophan synthase (DMATS) gene from a fungal Neosartorya sp. was cloned and overexpressed as a soluble His6-fusion protein in Escherichia coli. The enzyme was found to catalyze the prenylation of l-tryptophan at the C7 position of the indole moiety in the presence of dimethylallyl diphosphate; thus, it functions as a 7-DMATS. In this study, we describe the biochemical characterization of 7-DMATS from Neosartorya sp., referred to as 7-DMATSNeo, and the structural basis of the regioselective prenylation of l-tryptophan at the C7 position by comparison of the three-dimensional structural models of 7-DMATSNeo with FgaPT2 (4-DMATS) from Aspergillus fumigatus. |
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| Keywords: | 7-Dimethylallyl tryptophan synthase (7-DMATS) Prenylated indole derivatives Regioselective prenylation Three-dimensional structural models |
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