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Activity-based Proteomics of Enzyme Superfamilies: Serine Hydrolases as a Case Study

2010; Elsevier BV; Volume: 285; Issue: 15 Linguagem: Inglês

10.1074/jbc.r109.097600

1083-351X

Gabriel M. Simon, Benjamin F. Cravatt,

Chemical Synthesis and Analysis

Genome sequencing projects have uncovered thousands of uncharacterized enzymes in eukaryotic and prokaryotic organisms. Deciphering the physiological functions of enzymes requires tools to profile and perturb their activities in native biological systems. Activity-based protein profiling has emerged as a powerful chemoproteomic strategy to achieve these objectives through the use of chemical probes that target large swaths of enzymes that share active-site features. Here, we review activity-based protein profiling and its implementation to annotate the enzymatic proteome, with particular attention given to probes that target serine hydrolases, a diverse superfamily of enzymes replete with many uncharacterized members.