Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III

A Matić, F Šupljika, H Brkić, J Jurasović… - International journal of …, 2023 - mdpi.com
Dipeptidyl peptidase III (DPP III, EC 3.4. 14.4) is a monozinc metalloexopeptidase that
hydrolyzes dipeptides from the N-terminus of peptides consisting of three or more amino …

Preparation and characterization of cobalt-substituted anthrax lethal factor

CE Säbel, R Carbone, JR Dabous, SY Lo… - Biochemical and …, 2011 - Elsevier
Anthrax lethal factor (LF) is a zinc-dependent endopeptidase involved in the cleavage of
mitogen-activated protein kinase kinases near their N-termini. The current report concerns …

High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue

SY Lo, CE Säbel, MI Webb, CJ Walsby… - Journal of Inorganic …, 2014 - Elsevier
Anthrax lethal factor (LF) is a zinc-dependent metalloendopeptidase and a member of the
gluzincin family. The current report demonstrates a high metal substitution tolerance of LF …

An investigation of the pH dependence of copper-substituted anthrax lethal factor and its mechanistic implications

CJ Young, K Richard, A Beruar, SY Lo… - Journal of Inorganic …, 2018 - Elsevier
Anthrax lethal factor (LF) is a zinc-dependent endopeptidase involved in the cleavage of
proteins critical to the maintenance of host signaling pathways during anthrax infections …

Specificity-directed design of a FRET-quenched heptapeptide for assaying thermolysin-like proteases

DL Goulet, U Fraaz, CJ Zulich, TJ Pilkington… - Analytical …, 2020 - Elsevier
Thermolysin (TL) is an industrially important zinc endopeptidase, and the prototype of the
M4 family of metallopeptidases. The catalytic function of TL and its relatives is typically …

[HTML][HTML] Influence of chemical denaturants on the activity, fold and zinc status of anthrax lethal factor

SY Lo, CE Säbel, JPJ Mapletoft, S Siemann - Biochemistry and Biophysics …, 2015 - Elsevier
Anthrax lethal factor (LF) is a zinc-dependent endopeptidase which, through a process
facilitated by protective antigen, translocates to the host cell cytosol in a partially unfolded …

Highly dynamic metal exchange in anthrax lethal factor involves the occupation of an inhibitory metal binding site

CJ Young, S Siemann - Chemical Communications, 2016 - pubs.rsc.org
Metal exchange is a common strategy to replace the zinc ion of many zinc proteins with
other transition metals amenable to spectroscopic investigations. We here demonstrate that …

[HTML][HTML] Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor

LH Montpellier, S Siemann - FEBS letters, 2013 - Elsevier
Translocation of the zinc-dependent metalloendopeptidase anthrax lethal factor (LF) from
the endosome to the cytosol requires an acidic endosomal milieu. In the current study, we …

Vezanje iona prijelaznih metala u ljudskoj dipeptidil-peptidazi III

A Matić - 2024 - repozitorij.unizg.hr
Sažetak Cilj istraživanja bio je odrediti učinak vezanja različitih dvovalentnih iona metala:
Zn2+, Mn2+, Co2+, Cu2+, u različitim koncentracijama, na aktivnost ljudske dipeptidil …

Effect of pH and denaturants on the fold and metal status of anthrax lethal factor

SY Lo, DL Goulet, U Fraaz, S Siemann - Archives of Biochemistry and …, 2020 - Elsevier
Anthrax lethal factor (LF) is a critical component of the anthrax toxin, and functions
intracellularly as a zinc-dependent endopeptidase targeting proteins involved in maintaining …