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Discovery of a non-canonical prototype long-chain monoacylglycerol lipase through a structure-based endogenous reaction intermediate complex
Citation Link: https://doi.org/10.15480/882.8928
Publikationstyp
Journal Article
Date Issued
2023-11-27
Sprache
English
Author(s)
Pinotsis, Nikos
Tomas, Nicolas
Chatziefthymiou, Spyros D.
Litz, Claudia
Mortensen, Simon Arnold
Daffé, Mamadou
Marrakchi, Hedia
TORE-DOI
Journal
Volume
14
Issue
1
Article Number
7649
Citation
Nature Communications 14 (1): 7649 (2023-11-27)
Publisher DOI
Scopus ID
Publisher
Springer
The identification and characterization of enzyme function is largely lacking behind the rapidly increasing availability of large numbers of sequences and associated high-resolution structures. This is often hampered by lack of knowledge on in vivo relevant substrates. Here, we present a case study of a high-resolution structure of an unusual orphan lipase in complex with an endogenous C18 monoacylglycerol ester reaction intermediate from the expression host, which is insoluble under aqueous conditions and thus not accessible for studies in solution. The data allowed its functional characterization as a prototypic long-chain monoacylglycerol lipase, which uses a minimal lid domain to position the substrate through a hydrophobic tunnel directly to the enzyme’s active site. Knowledge about the molecular details of the substrate binding site allowed us to modulate the enzymatic activity by adjusting protein/substrate interactions, demonstrating the potential of our findings for future biotechnology applications.
DDC Class
660: Chemistry; Chemical Engineering
Publication version
publishedVersion
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s41467-023-43354-4.pdf
Type
Main Article
Size
2.23 MB
Format
Adobe PDF