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Class Assignment of Sequence‐Unrelated Members of Enzyme Superfamilies by Activity‐Based Protein Profiling
Author(s) -
Jessani Nadim,
Young Jason A.,
Diaz Sandra L.,
Patricelli Matthew P.,
Varki Ajit,
Cravatt Benjamin F.
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200463098
Subject(s) - serine , serine hydrolase , enzyme , biochemistry , superfamily , peptide sequence , chemistry , hydrolase , multiple sequence alignment , profiling (computer programming) , homology (biology) , biology , sequence alignment , computational biology , amino acid , gene , computer science , operating system
No longer in a class of its own : By using a gel‐free platform for activity‐based protein profiling (ABPP; see figure), it was shown that the enzyme sialic acid 9‐ O ‐acetylesterase (SAE), which shares no sequence homology with other enzymes, is a member of the serine hydrolase superfamily. The site of fluorophosphonate labeling in SAE was identified as serine 127; this residue is essential for catalytic activity.