Catechol Oxidase Activity of Di-Cu2+-Substituted Aminopeptidase from Streptomyces griseus
Journal of the American Chemical Society2005Vol. 127(47), pp. 16380–16381
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Abstract
Streptomyces griseus aminopeptidase exhibits activities toward the hydrolyses of peptides and bis(p-nitrophenyl)phosphate (40 billion fold) and catechol oxidation reported herein with catalytic efficiency (kcat/Km) only about 10 times smaller than that of gypsywort catechol oxidase. The multifunctionality of this enzyme suggests that it is a unique system for further exploration of protein structure and function and a template for design of enzymes of diverse activities.
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