Saturation mutagenesis on Arg244 of the tryptophan C4-prenyltransferase FgaPT2 leads to enhanced catalytic ability and different preferences for tryptophan-containing cyclic dipeptides

• Published in: Applied microbiology and biotechnology Vol. 100; no. 12; pp. 5389 - 5399
• Main Authors: Fan, Aili, Li, Shu-Ming
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.06.2016; Springer; Springer Nature B.V
• Subjects: Alkylation; Amino acids; Arginine - genetics; Aspergillus fumigatus; Aspergillus fumigatus - enzymology; Aspergillus fumigatus - metabolism; Binding sites; Biocatalysis; Biocatalysts; Biomedical and Life Sciences; Biosynthesis; Biotechnologically Relevant Enzymes and Proteins; Biotechnology; catalytic activity; Cyclic dipeptides; Cytotoxicity; Dimethylallyltranstransferase - genetics; Dimethylallyltranstransferase - isolation & purification; Dimethylallyltranstransferase - metabolism; dipeptides; Dipeptides - metabolism; E coli; Enzymes; Ergot; Ergot Alkaloids; Experiments; Friedel-Crafts reaction; Fungi; Genetic aspects; Kinetics; Life Sciences; Magnetic Resonance Spectroscopy; Metabolites; Microbial Genetics and Genomics; Microbiology; Mutagenesis; mutants; Natural products; Peptides; Physiological aspects; Plasmids; Prenylation; Proteins; Saturation mutagenesis; Studies; Substrate Specificity; Transferases; Tryptophan; Turnover rate; Cyclic dipeptide; Prenyltransferase; Friedel–Crafts alkylation; Enzyme catalysis; Saturation mutagenesis; Dimethylallyltryptophan synthase

FgaPT2 from Aspergillus fumigatus catalyzes a Friedel–Crafts alkylation at C-4 of l -tryptophan and is involved in the biosynthesis of the ergot alkaloids fumigaclavines. Several tryptophan-containing cyclic dipeptides had also been prenylated by FgaPT2, but the turnover rate ( k cat ) was low. Here...