[Studies of the consecutive hydrolysis of dipeptidyl-4-(phenylazo)-phenylamides by an aminopeptidase from Brassica napus].
The relatively alanine-specific amino peptidase from Brassica napus hydrolyzes dipeptidyl-4-(phenylazo)-phenylamide according to a consecutive mechanism. Enzyme-kinetic studies of dipeptidyl-4-(phenylazo)-phenylamides carried out by means of spectrometrical procedures of measurement are only possible when the increase in the concentration of the fission product p-aminoazobenzene is recorded. For assessing the kinetic parameters of the intermediary steps of the hydrolysis of dipeptidyl-4-(phenylazo)-phenylamides a function is derived describing the dependence of the concentration of fission products of p-aminoazobenzene on reaction time. The satisfactory correspondence of the kinetic parameters calculated for the intermediary-originating substrate L-ala-4-(phenylazo)-phenylamide as substrate demonstrates the applicability of the procedure described in the present paper.
D000626:Aminopeptidases / Q000378:metabolism*; D000814:Aniline Compounds / Q000378:metabolism*; D001391:Azo Compounds; D001937:Brassica / Q000201:enzymology*; D004151:Dipeptides / Q000378:metabolism; D004590:Electrophoresis, Paper; D006868:Hydrolysis; D008956:Models, Chemical; D010128:p-Aminoazobenzene / Q000378:metabolism
D000814:Aniline Compounds; D001391:Azo Compounds; D004151:Dipeptides; D010128:p-Aminoazobenzene; D000626:Aminopeptidases
Untersuchungen zur konsekutiven Hydrolyse von Dipeptidyl-4-(phenylazo)-phenylamiden durch eine Aminopeptidase aus Brassica napus.