Journal
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volume 18, Issue 6, Pages 463-473Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/14756360310001605543
Keywords
DAO; kidney diamine oxidase; substrate inhibition
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Pig kidney diamine oxidase (DAO) and other semicarbazide-sensitive amine oxidases (SSAO) show clear substrate-inhibition kinetics and a reaction-scheme mechanism based on two substrate binding sites. We evaluated several reaction scheme mechanisms with a non-linear regression program (NCSS), estimating R-2 , the constants of the equations and their standard errors and we determined the deviation of experimental data from theoretical equations. The best fit was obtained with a dead end mechanism with two binding sites. Based on this scheme, other schemes for a two-substrate reaction and for mechanisms of inhibition were constructed. These reaction schemes, even at low substrate concentration, fitted experimental data better than Michaelis-Menten kinetics, and provided information on the mechanisms of action of inhibitors. The presence of two substrate-binding sites on pig kidney DAO was confirmed by all experimental data.
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