Catechol Oxidase Activity of Di-Cu2+-Substituted Aminopeptidase from Streptomyces griseus
J. Am. Chem. Soc. 2005, 127, 16380-16381.

Giordano F. Z. da Silva and Li-June Ming*
Department of Chemistry and Institute for Biomolecular Science, University of South Florida, 4202 E. Fowler Avenue, Tampa, Florida 33620-5250

Streptomyces griseus aminopeptidase exhibits activities toward the hydrolyses of peptides and bis(p-nitrophenyl)phosphate (40 billion folds), and catechol oxidation reported herein with catalytic efficiency kcat/Km only about 10 times smaller than that of gypsywort catechol oxidase.  The multi-functionality 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.

(reprint in pdf)

CuCuSgAP at crossroads