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The **serine hydrolase-like protein (SERHL)**, encoded by the _SERHL_ gene, is an alpha/beta-hydrolase fold enzyme containing a conserved catalytic triad (often serine-histidine-aspartate) and a peroxisomal targeting signal[2]. It is upregulated in mouse skeletal muscle in response to passive mechanical stretch and may contribute to skeletal muscle hypertrophy by influencing peroxisomal function and/or metabolic signaling pathways. Like other serine hydrolases, SERHL catalyzes the hydrolytic cleavage of specific substrate bonds (esters, thioesters, amides). The precise endogenous substrates and physiological roles of SERHL are not completely characterized, but it is part of a large superfamily with diverse roles in metabolism, neurotransmission, inflammation, and diseases such as cancer and infection[2][1][4].
Drugs targeting serine hydrolases generally act by covalently binding the active site serine, leading to enzyme inhibition (mechanism-based inactivators)
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