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Updated: Aug 14, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus
Giordano F Z da Silva1, Li-June Ming
1Department of Chemistry and Institute for Biomolecular Science, University of South Florida, 4202 East Fowler Avenue, Tampa, Florida 33620-525, USA.
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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