Structure-based protein engineering enables prenyl donor switching of a fungal aromatic prenyltransferase

• Published in: Organic & biomolecular chemistry Vol. 16; no. 40; pp. 7461 - 7469
• Main Authors: Mai, Peter, Zocher, Georg, Stehle, Thilo, Li, Shu-Ming
• Format: Journal Article
• Language: English
• Published: CAMBRIDGE Royal Soc Chemistry 17.10.2018; Royal Society of Chemistry
• Subjects: Catalysis; Chemistry; Chemistry, Organic; Data processing; Donors (electronic); Enzymes; Fungi; Hydrophobicity; Microorganisms; Molecular modelling; Molecular structure; Mutagenesis; NMR; Nuclear magnetic resonance; Physical Sciences; Prenyltransferases; Primers; Protein engineering; Protein structure; Proteins; Saturation mutagenesis; Science & Technology; Selectivity; Site-directed mutagenesis; SYNTHASE; PHEROMONE; PROMISCUITY; NATURAL-PRODUCTS; SUBSTRATE; ENZYMES; SERVER; CATALYTIC MECHANISM

Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few...