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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