A Superfamily-wide Activity Atlas of Serine Hydrolases in <i>Drosophila melanogaster</i>.
Ontology highlight
ABSTRACT: The serine hydrolase (SH) superfamily is, perhaps, one of the largest functional enzyme classes in all forms of life and consists of proteases, peptidases, lipases, and carboxylesterases as representative members. Consistent with the name of this superfamily, all members, without any exception to date, use a nucleophilic serine residue in the enzyme active site to perform hydrolytic-type reactions via a two-step ping-pong mechanism involving a covalent enzyme intermediate. Given the highly conserved catalytic mechanism, this superfamily has served as a classical prototype in the development of several platforms of chemical proteomics techniques, activity-based protein profiling (ABPP), to globally interrogate the functions of its different members in various native, yet complex, biological
SUBMITTER: Kumar K
PROVIDER: S-EPMC7610703 | biostudies-literature | 2021 Apr
REPOSITORIES: biostudies-literature
ACCESS DATA