Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 15, Pages 11051-11055Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R109.097600
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Funding
- National Institutes of Health [CA087660, CA132630, DA025285]
- ARCS Foundation
- Koshland Graduate Fellowship in Enzyme Biochemistry
- Skaggs Institute for Chemical Biology
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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.
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