Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus.
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.
da Silva
Giordano F Z
GF
Department of Chemistry and Institute for Biomolecular Science, University of South Florida, 4202 East Fowler Avenue, Tampa, Florida 33620-525, USA.
Ming
Li-June
LJ
D000626:Aminopeptidases / Q000737:chemistry* / Q000378:metabolism; D004156:Catechol Oxidase / Q000737:chemistry / Q000378:metabolism*; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D013305:Streptomyces griseus / Q000201:enzymology*
D003300:Copper; D004156:Catechol Oxidase; D000626:Aminopeptidases