Aminopeptidase

Aminopeptidases are enzymes that catalyze the cleavage of single amino acids from the N -terminal end of a protein. Aminopeptidases are present in all living things. In humans, have been discovered about 20 of them. Except for protein maturation, they serve in the human metabolism and the regulation of peptide hormone levels and the digestion of proteins in the intestine.

Aminopeptidases belong to the group of exopeptidases, ie the protein-splitting enzymes that work on proteins of terminal peptide bonds. In most cases include aminopeptidases to the metalloproteases. All natural amino acids is specific aminopeptidases which only that cleave at the N -terminus of a protein (arginine aminopeptidase, leucine aminopeptidase, etc.). Many of these enzymes are tightly bound to the cell wall.

Catalyzed reactions

Peptidases break down proteins by hydrolysis of the peptide bonds. While endopeptidases cleave proteins within their molecules break down these exopeptidases from " molecule edge " her. Aminopeptidase specifically attack the N-terminal or amino -terminal end of the peptides and thereby cleave a single amino acid from ( as aminoacyl- peptide hydrolases and iminoacyl peptide hydrolases ).

Industrial Application

Aminopeptidase can be used in the enzymatic kinetic resolution of DL-2- Arylglycinamiden. When using a L- aminopeptidase as catalyst, the L-2- Arylglycinamid is enantioselectively hydrolysed to L-2- aryl glycine, while D -2- Arylglycinamid remains unchanged.