Hydrolysis of amide bonds by metal complexes has been of great interest since it was
revealed that the active site of carboxypeptidase A contains a zinc ion [1]. The task of …

An immobile artificial metallopeptidase having a well-defined active site was constructed on
the backbone of cross-linked polystyrene by adjoining a guanidinium moiety to the Cu (II) …

In our previous research we demonstrated the sequence specific peptide bond hydrolysis of
the R 1-(Ser/Thr)-Xaa-His-Zaa-R 2 in the presence of Ni (II) ions. The molecular mechanism …

Metal ions and complexes that hydrolyze peptides and proteins have become increasingly
important in recent years. These reagents have shown great promise for use in a variety of …

The ability of a metal ion to cooperate with various inter-and intramolecular acids and bases
andpromote amide hydrolysis has been investigated. Phenolic and carboxylic functional …

The rate of intramolecular amide hydrolysis in substitutionally inert Co (III) complexes has
been investigated. In these models for zinc-containing peptidases, such as …

The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which
bound sequentially at two distinct sites. Both the mono-and disubstituted forms of AAP …

In this density functional theory study, reaction mechanisms of a co-catalytic binuclear metal
center (Zn1–Zn2) containing enzyme leucine aminopeptidase for two different metal …

Three thioamide peptides in which the oxygen atom of the scissile peptide bond is replaced
by sulfur (denoted by (= S)) were synthesized and found to be good, convenient substrates …

Conspectus The selective hydrolysis of a peptide or amide bond (−(O) C–NH−) by a
synthetic metallopeptidase is required in a wide range of biological, biotechnological, and …