Open AccessSteady‐State Kinetic Studies on Benzylamine Oxidase from Pig Plasma
Author(s) -
KELLY Iain D.,
KNOWLES Peter F.,
YADAV Kapil D. S.,
BARDSLEY William G.,
LEFF Paul,
WAIGHT Roy D.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06183.x
Subject(s) - benzylamine , substrate (aquarium) , chemistry , imidazole , steady state (chemistry) , enzyme , amine gas treating , ammonia , kinetics , catalysis , oxidase test , stereochemistry , biochemistry , medicinal chemistry , organic chemistry , biology , ecology , physics , quantum mechanics
Steady‐state kinetic studies on the enzyme benzylamine oxidase from pig plasma are described. Eadie‐Hofstee plots with benzylamine as the varying substrate are non‐linear; examination of this data indicates that the observed effects are probably due to the amine substrate participating in at least two reactions with enzyme. Ammonia and imidazole modify the activity of the enzyme; under specified conditions of pH or modifier concentration, the effect on the activity can be either activation or inhibition. Eadie‐Hofstee plots of the data establish that the modifier also participates in at least three reactions with the enzyme. Eadie‐Hofstee plots at pH 9 with oxygen as the varying substrate are linear, which allows kinetic parameters to be determined. From studies on the effect of ammonia and imidazole on these parameters, information has been derived on how these modifiers affect component steps of the catalytic cycle.