aminopeptidases

All Noun
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  • Work within the past two decades has provided vital knowledge regarding the mechanisms of aminopeptidases.
  • Aminopeptidases play a role in the metabolism of several peptides that may be involved in blood pressure and the pathogenesis of essential hypertension.
  • Some aminopeptidases are monomeric, and others are assemblies of relatively high mass (50 kDa) subunits.
  • Aminopeptidases function as exopeptidases which remove amino acids from the amino-terminus of proteins.
  • One of the functions of aminopeptidases is to degrade potentially toxic peptides in the cytosol.
  • Aminopeptidases also contributes an aroma in traditional Norman Camembert.
  • CDNA sequences are available for several aminopeptidases and a crystal structure of the open state of human endoplasmic reticulum Aminopeptidase 1 ERAP1 is presented here.
  • Papain belongs to a family of related proteins with a wide variety of activities, including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity.
  • Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates.
  • Geotrichum candidum reduces the bitterness in Camembert cheese through the activity of the aminopeptidases that hydrolyze low molecular weight hydrophobic peptides.
  • Aminoptidase activity is also luminal in the posterior midgut, but cellular aminopeptidases are required for peptide processing in both anterior and posterior midguts.
  • Erepsin may contain dipeptidases, aminopeptidases and occasionally carboxypeptidases, and is often grouped under exopeptidases, proteases that work only on the outermost peptide bonds of a polypeptide chain.
  • Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein (N-terminus) or peptide substrates.
  • Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins.
  • Furthermore the activity of the enzyme is inhibited by o-phenanthroline, a metalloprotease inhibitor and by arphamenine A, a potent inhibitor of aminopeptidases such as LTA4H.
  • The K48-linked polyubiquitination is a marker for proteasomal degradation that releases 2 to 24 amino acid-long peptides, which are quickly degraded to amino acids by various oligopeptidases and aminopeptidases present in the cytoplasm.
  • Some detach the terminal amino acids from the protein chain (exopeptidases, such as aminopeptidases, carboxypeptidase A); others attack internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase).
  • XPNPEP3 belongs to a family of X-pro-aminopeptidases (EC 3.4.11.9) that utilize a metal cofactor and remove the N-terminal amino acid from peptides with a proline residue in the penultimate position.