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5'-O-(L-Serylsulfamoyl)adenosine is a synthetic small molecule analog of the aminoacyl adenylate intermediate formed during protein synthesis. It consists of an adenosine moiety linked via a stable sulfamoyl bond to an L-serine residue. This compound acts as a non-hydrolyzable mimic of seryl adenylate and functions as a potent inhibitor of seryl-tRNA synthetase (SerRS), an essential enzyme in protein translation that catalyzes the attachment of serine to its cognate tRNA. By occupying the active site of SerRS and mimicking the natural reaction intermediate, it blocks aminoacylation and thus inhibits protein synthesis. The compound is primarily used in biochemical research to study enzyme mechanisms and for structure-based drug design targeting aminoacyl-tRNA synthetases[1][9].
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