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Proteases
Proteases (also known as peptidases or proteinases) are a subgroup of hydrolase enzymes that catalyze the cleavage of peptide bonds within proteins. Proteases have traditionally been classified into serine, cysteine, aspartic, and metallopeptidases with more recently three categories added: N-terminal threonine peptidases, glutamate peptidases, and asparagine peptidases. Proteases are further divided into endopeptidases and exopeptidases, which cut in the middle or at the ends of substrates, the latter being further classified into aminopeptidases and carboxypeptidases, which cleave off N-terminal and C-terminal amino acids. Proteases target peptide bonds of proteins and peptides and some catalyze extensive protein-processing events such as the digestion or degradation of intake proteins and the development and remodeling of tissues.
Further reading
Barrett and McDonald (1986) Nomenclature: protease, proteinase and peptidase. Biochem.J. 237(3) 935 PMID: 3541905
Rawlings and Bateman (2019) Origins of peptidases. Biochimie 166 4 PMID: 31377195
Nguyen et al (2019) Distributions of Extracellular Peptidases Across Prokaryotic Genomes Reflect Phylogeny and Habitatat. Front. Microbiol. 10 413 PMID: 30891022
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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