منابع مشابه
Aspartic proteinases and their inhibitors.
Proteolytic enzymes are classified on the basis of their catalytic mechanism as belonging to one of four groups: the serine, cysteine, metallo and aspartic proteinases (Kay, 1982). In contrast to the detailed sequence information and three-dimensional structures that have been produced for many enzymes belonging to the first three groups, relatively little is known about the aspartic proteinase...
متن کاملStructure and function of plant aspartic proteinases.
Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues indispensible for catalytic activity. The three-dimensional structure of two plant aspartic proteinases has been determined, sharing significant structural...
متن کاملProchymosin activation by non-aspartic proteinases.
Prochymosin can be converted into chymosin by an action of external proteinases. Thus, thermolysin at pH 5.05 converts calf prochymosin into active Phe-chymosin, which is one amino acid longer than chymosin from the N-terminus with a yield of 73%. Even better results were achieved with prochymosin activation by Legionella pneumophila metalloproteinase. Apparently the stretch of prochymosin poly...
متن کاملAspartic proteinases in the digestive tract of marine decapod crustaceans.
Decapod crustaceans synthesize highly active proteolytic enzymes in the midgut gland and release at least a part of them into the stomach where they facilitate the first step in peptide hydrolysis. The most common proteinases in the gastric fluid characterized so far are serine proteinases, that is, trypsin and chymotrypsin. These enzymes show highest activities at neutral or slightly alkaline ...
متن کاملA systematic series of synthetic chromophoric substrates for aspartic proteinases.
The hydrolysis of the chromogenic peptide Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu at the Phe-Phe(4-NO2) bond by nine aspartic proteinases of animal origin and seven enzymes from micro-organisms is described [Phe(4-NO2) is p-nitro-L-phenylalanine]. A further series of six peptides was synthesized in which the residue in the P3 position was systematically varied from hydrophobic to hydrophilic. The Ph...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1984
ISSN: 0014-5793
DOI: 10.1016/0014-5793(84)81085-6