Kinetics of Hydrolysis of NαBenzoyl-p-Guanidino-L-PhenylaIaiiine p-Nitroanilide by Trypsin
- 1 July 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 94 (1) , 123-128
- https://doi.org/10.1093/oxfordjournals.jbchem.a134320
Abstract
A new chromogenic substrate, Nα-benzoyl-p-guarudino-L-phenylalanine p-nitro-anilide (Bz-GPA-pNA), was synthesized. This compound is a good substrate for bovine trypsin (Km=1.56 × 10−6 M, kcat = 0.081 S−1, at pH 8.2) and was hydrolyzed as fast as Nα-benzoyl-L-arginine p-nitroanilide (Bz-Arg-pNA) with much the same kcat/Km values. But the values are two orders of magnitude smaller than those for ester substrates, Nα-benzoyl-p-guanidino-L-phenylalanine ethyl ester (Bz-GPA-OEt) and Nα-benzoyl-L-arginine ethyl ester (Bz-Arg-OEt). Substrate activation behavior was observed on tryptic hydrolysis of this new substrate in a substrate concentration range higher than about 5.0 × 10−4 M in analogy with the trypsin-Bz-Arg-pNA system.Keywords
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