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Activity-based Proteomics of Enzyme Superfamilies: Serine Hydrolases as a Case Study
Open accessAbstract
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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Cites
Global analysis of protein localization in budding yeast
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2-Arachidonoylgylcerol: A Possible Endogenous Cannabinoid Receptor Ligand in Brain
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A Comprehensive Profile of Brain Enzymes that Hydrolyze the Endocannabinoid 2-Arachidonoylglycerol
Blankman, J. L., Simon, G. M., & Cravatt, B. F. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.11.006 · Cited by 1,177
Self-citationMonoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
Nomura, D. K., Long, J. Z., Niessen, S., Hoover, H. S., Ng, S.-W., & Cravatt, B. F. (2010) · Cell · doi:10.1016/j.cell.2009.11.027 · Cited by 1,002
Self-citationBöttcher, T., & Sieber, S. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8051365 · Cited by 207
Cited by
The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease
Long, J. Z., & Cravatt, B. F. (2011) · Chemical Reviews · doi:10.1021/cr200075y · Cited by 425
Self-citationClick Chemistry in Proteomic Investigations
Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 380
Chemical Probes of Endocannabinoid Metabolism
Blankman, J. L., & Cravatt, B. F. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.006387 · Cited by 327
Self-citationBachovchin, D. A., Ji, T., Li, W., Simon, G. M., Blankman, J. L., Adibekian, A., Hoover, H., Niessen, S., & Cravatt, B. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011663107 · Cited by 274
Self-citationHow Chemoproteomics Can Enable Drug Discovery and Development
Moellering, R. E., & Cravatt, B. F. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.001 · Cited by 182
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Metadata
- Authors
- Simon, G. M., & Cravatt, B. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 285
- Issue
- 15
- Pages
- 11051-11055
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2052023845
- Cited by
- 325
- References
- 6
- FWCI
- 10.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
