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Arginyl aminopeptidase-like 1 (RNPEPL1) is a broad specificity metalloaminopeptidase and member of the M1 family of zinc metallopeptidases that preferentially hydrolyzes N-terminal methionine, citrulline, or glutamine residues from peptides. RNPEPL1 is ubiquitously expressed across human tissues and displays a broad range of enzymatic activity, with highest activity at neutral to slightly alkaline pH. The enzyme has similarities to leukotriene A4 hydrolase and clusters phylogenetically with proteins involved in inflammation, though its biological role remains incompletely defined; evidence suggests a modest decrease in expression during inflammatory responses. No approved therapeutic agents target RNPEPL1, and its involvement in human diseases remains under investigation.
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