Abstract
The substrate specificity of and effect of inhibitors on potato tuber phenolase are described. For a particular inhibitor, K i depends upon whether an o-dipbenol or monophenol is used as substrate, and thus it is proposed that different protein molecules are responsible for the oxidation of o-diphenols and the hydroxylation of monophenols. A study of the substrate specificity of the enzyme suggests that the monophenol hydroxylase activity has no biosynthetic significance and that the main function of the enzyme is to provide a defence against wounding and infection by the oxidation of chlorogenic acid.
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