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- W2308869884 abstract "Activity-based protein profiling identifies AIG1 and ADTRPP as transmembrane threonine hydrolases with substrates that include several fatty acid esters of hydroxyl fatty acids (FAHFAs). New inhibitors of these enzymes inhibit FAHFA hydrolysis. Enzyme classes may contain outlier members that share mechanistic, but not sequence or structural, relatedness with more common representatives. The functional annotation of such exceptional proteins can be challenging. Here, we use activity-based profiling to discover that the poorly characterized multipass transmembrane proteins AIG1 and ADTRP are atypical hydrolytic enzymes that depend on conserved threonine and histidine residues for catalysis. Both AIG1 and ADTRP hydrolyze bioactive fatty acid esters of hydroxy fatty acids (FAHFAs) but not other major classes of lipids. We identify multiple cell-active, covalent inhibitors of AIG1 and show that these agents block FAHFA hydrolysis in mammalian cells. These results indicate that AIG1 and ADTRP are founding members of an evolutionarily conserved class of transmembrane threonine hydrolases involved in bioactive lipid metabolism. More generally, our findings demonstrate how chemical proteomics can excavate potential cases of convergent or parallel protein evolution that defy conventional sequence- and structure-based predictions." @default.
- W2308869884 created "2016-06-24" @default.
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- W2308869884 date "2016-03-28" @default.
- W2308869884 modified "2023-10-18" @default.
- W2308869884 title "AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs" @default.
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- W2308869884 doi "https://doi.org/10.1038/nchembio.2051" @default.
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