aminopeptidase

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a·mi·no·pep·ti·dase

 (ə-mē′nō-pĕp′tĭ-dās′, -dāz′, ăm′ə-)
n.
Any of various enzymes that catalyze the hydrolysis of the terminal peptide bond of a polypeptide from the end that contains a free amino group.

aminopeptidase

(əˌmiːnəʊˈpɛptɪˌdeɪz)
n
an enzyme produced by the glands of the small intestine
References in periodicals archive ?
Differential alteration of two aminopeptidases N associated with resistance to Bacillus thuringiensis toxin Cry1Ac in cabbage looper.
Although bradykinin is degraded by other peptidases--for example, aminopeptidases M, carboxypeptidases N, neutral endopeptidases, dipeptidyl peptidase IV, enkephalinases, or neprilysin--these enzymes are less effective than ACE (7).
The use of a non-specific technique (Walter, 1984) at a neutral and basic pH enables the quantification of activities of different proteases, such as trypsin, chymotrypsin, carboxypeptidases, aminopeptidases, elastases and collagenases as the main proteases that acts together as reported in several fish species (Torrissen, 1987; Klomklao, 2008; Unajak et al, 2012).
This post-translational modification (PTM) to pyroglutamate, present in many biologically active peptides and proteins, protects against degradation by aminopeptidases and in many cases determines functionality of protein or peptide (2-7).
A protease inhibitor cocktail containing proprietary concentrations of inhibitors with specificity for serine, cysteine, aspartic and aminopeptidases, but no metal-chelating agents that would inhibit MMPs (Sigma-Aldrich, St.
Tosedostat is a first-in-class selective inhibitor of aminopeptidases, which are required by tumour cells to provide amino acids necessary for growth and tumour cell survival, and is under development for the treatment of blood-related cancers.
Aminopeptidases catalyse the cleavage of amino acids from the amino-termini of protein or peptide substrates (8).
41] have isolated proteolytic species of Lactobacillus such as Lactobacillus bulgaricus and Lactobacillus rhamnosus with aminopeptidases and prolinase activity.
Domain III has a stalk region between residue 40 and residue 70, and after this residue there is a sequence WNXXRLP in APN, which is homologous to non-membrane bound aminopeptidases (32).
Two enzymes, called aminopeptidases, have been proposed as being responsible for releasing single amino acids from proteins, or peptides.
It is reported that the increase in free amino acids during the post-mortem storage of meat is caused by the action of aminopeptidases (Migita and Nishimura, 2006).
The APN showed the presence of the HEXXH zinc-binding motif (residues 355-359) characteristic of the zinc peptidases; the third zinc-binding ligand is also conserved in the sequence motif NEXFA (residues 377-381); the amino acid sequence shared the GAMEN motif(residues 319-323) which characterizes them as gluzincin aminopeptidases and involved in their aminopeptidase activity (Herrero et al.