Class Assignment of Sequence‐Unrelated Members of Enzyme Superfamilies by Activity‐Based Protein Profiling | Zendy

Jessani Nadim | Zendy; Young Jason A. | Zendy; Diaz Sandra L. | Zendy; Patricelli Matthew P. | Zendy; Varki Ajit | Zendy; Cravatt Benjamin F. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research