An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid...

An exopeptidase inhibitor is a drug that inhibits one or more exopeptidase enzymes. Exopeptidases are one of two types of proteases (enzymes that break...

nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids....

sequence is not necessary if exopeptidases are used to remove N-terminal His-tags (e.g., Qiagen TAGZyme). Furthermore, exopeptidase cleavage may solve the unspecific...

Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains...

involved are proteinases (cathepsins – B, D, H & L, and calpains) and exopeptidases (peptidase and aminopeptidase). These enzymes cause proteolysis of muscle...

endopeptidase genes and 69 exopeptidase genes, and A. sojae strain SMF134 has 83 endopeptidase genes and 67 exopeptidase genes. Similarly, starch-degrading...

is present in blood plasma and various body fluids. DPP-4 is a serine exopeptidase that cleaves X-proline or X-alanine dipeptides from the N-terminus of...

activity metallopeptidase activity metallocarboxypeptidase activity exopeptidase activity Cellular component cytoplasm integral component of membrane...

proteases (enzymes that break down proteins and peptides), the other being exopeptidases. Endopeptidases cleave peptide bonds of non-terminal amino acids (that...