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Implication of pH in the catalytic properties of anthrax lethal factor.

Abstract：

:The anthrax lethal factor (LF) is a Zn(2+)-endopeptidase specific for mitogen-activated protein kinase kinases (MAPKKs), which are cleaved within their N-terminal region. Much line of effort was carried out to elucidate the catalytic activity of LF for designing the inhibitor and to understand the cellular mechanism of its cytotoxicity. Current assay methods to analyze the LF activity have been based on a synthetic peptide, consisting of 15-20 residues around being cleaved. However, there are accumulating reports that the region distal to cleavage site is required for the LF-mediated proteolysis of substrate. In this study, we demonstrate the catalytic properties of LF, using the full-length native substrate, MEK. We described the catalytic properties of LF focused on the effects of the pH alteration, which was encountered during the endocytosis of lethal toxin, and of the requirement for metal ions. We present the first evidence that additional metal ions are required for the LF catalyzed hydrolysis of native substrate, and that the pH alteration causes a significant change of catalytic properties of LF.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kim J,Chai YG,Yoon MY

doi

10.1016/j.bbrc.2003.11.110

subject

Has Abstract

pub_date

2004-01-02 00:00:00

pages

217-22

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X03024811

journal_volume

313

pub_type

杂志文章

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