title: The hydrolysis by thermolysin of dipeptide derivatives that conatin substituted cysteine.
abstract: 1. The preparation of protected dipeptides of the form acetylglycylamino acid amides is described, where the amino acid is phenylalanine, leucine, valine, alanine, S-methylcysteine, S-ethylcysteine, S-benzylcysteine and S-phenylcysteine. 2. Kinetic parameters for the thermolytic hydrolysis of these blocked dipeptides are reported. The rate of hydrolysis was fastest when the amino acid was leucine or phenylalanine, slower when it was S-methylcysteine, valine or S-ethylcysteine, much slower when it was alanine, and negligible for S-phenylcysteine or S-benzylcysteine. 3. The results are compared with those for similar dipeptide derivatives with benzyloxycarbonyl and furylacryloyl blocking groups, which are hydrolysed faster.
mesh_terms: D000409:Alanine / Q000032:analysis; D000577:Amides / Q000032:analysis; D003460:Crystallization; D003545:Cysteine / Q000032:analysis; D004151:Dipeptides; D010450:Endopeptidases; D006868:Hydrolysis; D007700:Kinetics; D007930:Leucine / Q000032:analysis; D010649:Phenylalanine / Q000032:analysis; D013820:Thermolysin; D014633:Valine / Q000032:analysis
chemical_list: D000577:Amides; D004151:Dipeptides; D010649:Phenylalanine; D010450:Endopeptidases; D013820:Thermolysin; D007930:Leucine; D014633:Valine; D003545:Cysteine; D000409:Alanine