Serine proteases , as well as serine endopeptidases ( EC 3.4.21), are a group of enzymes that catalyze the process of degradation ( proteolysis ) of proteins to their constituent α-amino acid molecules by hydrolysis of the peptide bond . The main difference from other proteases is the presence of serine amino acids in its active center .
Serine proteases are found in both multicellular and unicellular organisms, both in eukaryotes and prokaryotes . They are divided into clans according to the structural features, and clans, in turn, are divided into families whose members have similar sequences.
Some serine endopeptidase inhibitors (for example, Narlaprevir ) have clinical significance, as they have the ability to inhibit the replication of viruses.
Literature
- “Analysis of the distribution and domain architecture of five families of serine proteases in eukaryotic genomes.” Tripathi LP, Sowdhamini R. Genome-wide survey of prokaryotic serine proteases: analysis of distribution and domain architectures of five serine protease families in prokaryotes (Eng.) // BMC Genomics : journal. - 2008 .-- Vol. 9 . - P. 549 . - DOI : 10.1186 / 1471-2164-9-549 . - PMID 19019219 .