Enzyme promiscuity receives remarkable attention in recent years, especially in terms of protein engineering for the design of efficient biocatalysts for desired/specific chemical reactions starting from promiscuous enzymes with similar catalytic machinery.<br/>In this context, we focused on an aza-Morita-Baylis-Hillman (aza-MBH) reaction, with products displaying anti-tumoral activity against human cervical cancer cells, with the aim of identifying enzymes showing promiscuous catalytic activity towards the selected reaction. We computationally screened protein data bank for naturally occurring enzymes with possible promiscuous activity using quantum mechanically optimized catalytic active sites models (theozymes). Hit proteins were evaluated first according to the positioning and interactions of the substrates in the active site, and then further investigated in solvated environment with molecular dynamic simulations.<br/>Screening protein databank successfully identified an enzyme with experimentally proved promiscuous activity.

Identification of promiscuous enzymes for the aza-Morita-Baylis-Hillman reaction

253rd National Meeting (2017)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.