A subclass of peptide hydrolases. They are classified primarily by their catalytic mechanism. Specificity is used only for identification of individual enzymes. They comprise the serine endopeptidases, EC 3.4.21; cysteine endopeptidases, EC 3.4.22; aspartic endopeptidases, EC 3.4.23, metalloendopeptidases, EC 3.4.24; and a group of enzymes yet to be assigned to any of the above sub-classes, EC 3.4.99. EC 3.4.-.
Enzymes that hydrolyse proteins (i.e. proteinases or peptidases), by cleaving peptide bonds within the protein chain, as opposed to exopeptidases, which remove amino acids from the ends of the chain.
Proteolytic enzymes that hydrolyse the peptide bonds of the terminal amino acids of proteins or peptides.
One of a group of enzymes that hydrolyze dietary proteins by breaking peptide bonds.
A digestive enzyme (e.g. pepsin) that splits a whole protein into small peptide fractions by splitting the linkages between peptides in the interior of the molecule.
A proteolytic enzyme that cleaves peptides in their centers rather than from their ends.