Disparate proteome reactivity profiles of carbon electrophiles.
Insights into the proteome reactivity of electrophiles are crucial for designing activity-based probes for enzymes lacking cognate affinity labels. Here, we show that different classes of carbon electrophiles exhibit markedly distinct amino acid labeling profiles in proteomes, ranging from selective reactivity with cysteine to adducts with several amino acids. These data specify electrophilic chemotypes with restricted and permissive reactivity profiles to guide the design of next-generation functional proteomics probes.
Weerapana
Eranthie
E
The Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Simon
Gabriel M
GM
Cravatt
Benjamin F
BF
D000596:Amino Acids / Q000737:chemistry*; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D015335:Molecular Probes / Q000737:chemistry*; D020543:Proteome / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*; D012680:Sensitivity and Specificity; D012697:Serine Endopeptidases / Q000737:chemistry*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D015335:Molecular Probes; D020543:Proteome; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases