Kinetic characterization of the Escherichia coli oligopeptidase A (OpdA) and the role of the Tyr607 residue-Reference-Cited by-同舟云学术

Kinetic characterization of the Escherichia coli oligopeptidase A (OpdA) and the role of the Tyr607 residue

Published:2010-08 Issue:2 Volume:500 Page:131-136
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Lorenzon Ricardo Z.,Cunha Carlos E.L.,Marcondes Marcelo F.,Machado Maurício F.M.,Juliano Maria A.,Oliveira Vitor,Travassos Luiz R.,Paschoalin Thaysa,Carmona Adriana K.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference33 articles.

1. Proteolysis in protein import and export: Signal peptide processing in eu-and prokaryotes

2. Proteolysis in Bacterial Regulatory Circuits

3. PROTEASES AND THEIR TARGETS IN ESCHERICHIA COLI

4. Localization and purification of two enzymes from Escherichia coli capable of hydrolyzing a signal peptide.

5. Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium

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2. YPTB3816 of Yersinia pseudotuberculosis strain IP32953 is a virulence-related metallo-oligopeptidase;BMC Microbiology;2016-11-25

3. Mycoplasma hyopneumoniae in vitro peptidase activities: Identification and cleavage of kallikrein-kinin system-like substrates;Veterinary Microbiology;2013-05

4. Oligopeptidase A;Handbook of Proteolytic Enzymes;2013