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.
Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus. Publishing Authors By Initials
Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of the American Chemical Society
VOLUME: 127
Page Numbers: 16380-1
Journal Abbreviation: J. Am. Chem. Soc.
ISSN: 0002-7863
DAY: 30
MONTH: Nov
YEAR: 2005
Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 7503056
Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus. Keywords Mesh Terms:
KEYWORDS: Streptomyces griseus
MESH TERMS: enzymology
Chemical & Substance for Abstract: Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus. Information
Substance Name: Aminopeptidases
Registry Number: EC 3.4.11.-
Grant and Affiliation Information for Catechol oxidase activity of di-Cu2+-substituted aminopeptidase from Streptomyces griseus.
AFFILIATION: Department of Chemistry and Institute for Biomolecular Science, University of South Florida, 4202 East Fowler Avenue, Tampa, Florida 33620-525, USA.
Country: United States
AGENCY: United States NIGMS
GRANT: GM064400-01A2
ACRONYM: GM
MEDLINETA: J Am Chem Soc
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