Benzyloxycarbonylphenylalanylcitrulline p-nitroanilide as a substrate for papain and other plant cysteine proteinases

After preliminary assays, with papain, bromelain and ficin, on a range of citrulline p-nitroanilides, values of Km and kcat. for the papain-catalysed hydrolysis of three derivatives, N alpha- benzyloxycarbonylcitrulline p-nitroanilide, benzyloxycarbonylphenylalanylcitrulline p-nitroanilide and benzy...

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Bibliographic Details
Published in:Biochemical journal 1984-04, Vol.219 (1), p.325-328
Main Authors: Gray, C J, Boukouvalas, J, Szawelski, R J, Wharton, C W
Format: Article
Language:English
Subjects:
Bromelains - metabolism
Citrulline - analogs & derivatives
Citrulline - metabolism
Dipeptides - metabolism
Ficain - metabolism
Hydrolysis
Kinetics
Oligopeptides - metabolism
Papain - metabolism
Plants - enzymology
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Summary:After preliminary assays, with papain, bromelain and ficin, on a range of citrulline p-nitroanilides, values of Km and kcat. for the papain-catalysed hydrolysis of three derivatives, N alpha- benzyloxycarbonylcitrulline p-nitroanilide, benzyloxycarbonylphenylalanylcitrulline p-nitroanilide and benzyloxycarbonylglycylphenylalanylcitrulline p-nitroanilide, were obtained. It is concluded that benzyloxycarbonylphenylalanylcitrulline p-nitroanilide is a highly selective substrate for the sensitive detection and assay of the plant cysteine proteinases.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2190325