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Leucine aminopeptidase Subject

Found to be subject to metal ion catalysis, but the discovery by Kroll in 1952 that the hydrolysis af a-amino acid esters was catalyzed by metal ions stimulated considerable interest in the area. Many of these reactions can be considered as simple model systems for such metalloenzymes as arboxypeptidase A, leucine aminopeptidase and glycylglycine dipeptidase.25... [Pg.415]

This discussion of the metalloexopeptidases has focused on the general role of these enzymes in the conversion of dietary proteins into amino acids. In particular, the apparent synergistic relationship which the pancreatic carboxypeptidases have with the major endopeptidases, trypsin, chymotrypsin, and pepsin, in order to facilitate formation of essential amino acids has been stressed. The chemical characteristics, metalloenzyme nature, and mechanistic details of a representative of each class of exopeptidase have been presented. Leucine aminopeptidase from bovine lens was shown to be subject to an unusual type of metal ion activation which may be representative of a more general situation. Carboxypeptidase A of bovine pancreas was discussed in terms of its three-dimensional structure, the implications of x-ray crystallography to mecha ... [Pg.238]

Cathepsins. Cathepsins are intracellular proteases of animal origin. The occurrence of several such enzymes has been demonstrated in various tissues, including spleen, pituitary gland, kidney, thymus, etc. It is obvious that there is no reason to anticipate that all cathepsins will have similar properties to each other or to any other proteases. Cathepsins have been designated by both Roman numerals and by letters. Some of these enzymes have been identified with enzymes purified independently, as cathepsin III with leucine aminopeptidase. Several are activated by sulfhydryl compounds, some by metals. The isolation of the various cathepsins and studies of their substrate specificities are subjects currently under investigation, but because of the lower concentration of enzyme in the source materials and the number of related enzymes present, this area of investigation has not reached the development of the study of digestive enzymes. [Pg.32]


See other pages where Leucine aminopeptidase Subject is mentioned: [Pg.221]    [Pg.213]    [Pg.431]    [Pg.21]   


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