Biology

Discovery of a non-canonical prototype long-chain monoacylglycerol lipase through a structure-based endogenous reaction intermediate complex

N. Pinotsis, A. Krüger, et al.

Explore the innovative research by Nikos Pinotsis and colleagues on the high-resolution structure of an orphan lipase in complex with a C18 monoacylglycerol ester. This groundbreaking study characterizes the enzyme's functionality and opens up exciting biotechnology applications through strategic modulation of enzyme-substrate interactions.

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Playback language: English

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Abstract

This study presents the high-resolution structure of an orphan lipase in complex with an endogenous C18 monoacylglycerol ester reaction intermediate. This allowed functional characterization as a prototypic long-chain monoacylglycerol lipase using a minimal lid domain to position the substrate. Modulation of enzymatic activity by adjusting protein/substrate interactions demonstrates the potential for biotechnology applications.

Publisher

Nature Communications

Published On

Nov 27, 2023

Authors

Nikos Pinotsis, Anna Krüger, Nicolas Tomas, Spyros D. Chatziefthymiou, Claudia Litz, Simon Arnold Mortensen, Mamadou Daffé, Hedia Marrakchi, Garabed Antranikian, Matthias Wilmanns

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