Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein (N-terminus) or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components. Aminopeptidases are used in essential cellular functions. Many, but ...
<enzyme> That remove the N terminal amino acid from a protein or peptide. ... (18 Nov 1997) ... 
Enzyme that cleaves amino acid residues from a protein chain commencing at the N-terminalEnzymes that remove the N-terminal amino acid from a protein or peptide.
Type: Term Pronunciation: ă-mē′nō-pep′ti-dāz Definitions: 1. Enzyme that catalyzes the breakdown of a peptide, removing the amino acyl residue at the amino end of the chain (an n-exopeptidase); found in intestinal secretions.(cytosol) Type: Term Pronunciation: ă-mē′nō-pep′ti-dās sī′tō-sol Definitions: 1. An enzyme of broad specificity, containing zinc, and catalyzing the hydrolysis of the N-terminal amino acyl group of a peptide (an exopeptidase).(microsomal) Type: Term Pronunciation: ă-mē′nō-pep′ti-dās mī-krō-sō′mal Definitions: 1. An aminopeptidase of broad specificity, but preferring n-terminal alanyl residues and discriminating against prolyl residues.
any of several intestinal hydrolytic enzymes that remove an amino acid from the end of a peptide chain having a free amino group. Cf. carboxypeptidase.