Enzymatic synthesis of chromogenic substrates for Glu,Asp-specific proteinases. |
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Authors: | E I Milgotina A S Shcheglov G B Lapa G G Chestukhina T L Voyushina |
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Institution: | V.M. Stepanov Laboratory of Protein Chemistry, Institute of Genetics and Selection of Industrial Microorganisms, Moscow, Russia. |
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Abstract: | Glu,Asp-specific endopeptidases represent a new subfamily of chymotrypsin-like proteolytic enzymes. These enzymes prefer Glu or Asp residues in the P1 position of the substrates. p-Nitroanilides of N-acylated di-, tri- and tetrapeptides with C-terminal glutamic or aspartic acid residues have been obtained. Acyl peptide p-nitroanilides were synthesized via acylation of glutamic or aspartic acid p-nitroanilides using methyl esters of the respective N-acylated peptides, generally with good yields. The reactions were performed in organic solvents using subtilisin 72 sorbed on silica as a catalyst. The kinetic parameters for the hydrolysis of these p-nitroanilides with proteinases from Bacillus intermedius and Bacillus licheniformis were determined. |
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