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 …

The chelation of protein-bound metal ions is typically thought to follow either a dissociative
(D) or an associative (A) path. While the former mechanism involves the spontaneous …

Matrix metalloproteinases (MMP) are an important family of proteases which catalyze the
degradation of extracellular matrix components. While the mechanism of peptide cleavage is …

Catalytic antibodies (catabodies) that degrade target antigens rapidly are rare. We describe
the metal-dependence of catabody construct 2E6, an engineered heterodimer of …

Matrix metalloproteinase-1 (MMP-1) plays crucial roles in disease-related physiologies and
pathological processes in the human body. We report here solution studies of MMP-1 …

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 …

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 …

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 …

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 …

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 …