Abstract
The variation of the rate of oxidation of histamine derivatives, diamines, a monoamine and aminoalkylonium compounds by pig kidney diamine oxidase with alteration of pH has been studied. Two types of behaviour of reaction velocity as a function of pH are shown; some substrates having a straightforward optimum pH value around pH 7·4 and others showing an uneven curve instead of a smooth maximum around this pH value. This could be related to inhibition by high substrate concentration as shown by the variation of substrate inhibition with pH. Implications of these findings in the interpretation of the mechanism of binding and oxidation of histamine derivatives by diamine oxidase are discussed. In particular, the side chain αβ dehydrogenation mechanism for the oxidation of histamine is criticised since histamine derivatives lacking β hydrogens were found to be substrates of DAO.
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