Dipeptidyl peptidase 3 (DPP3), a zinc‐dependent aminopeptidase, is a highly conserved
enzyme among higher animals. The enzyme cleaves dipeptides from the N‐terminus of tetra …

In what corresponds to a life span, metallocarboxypeptidases (MCPs) have jumped from
being mere contaminants in animal pancreas powders (in depression year 1929) to be key …

Human dipeptidyl-peptidase III (hDPP III) is a zinc-dependent hydrolase cleaving dipeptides
off the N-termini of various bioactive peptides. Thus, the enzyme is likely involved in a …

Carboxypeptidase A is a zinc-containing enzyme that cleaves the C-terminal residue in a
polypeptide substrate. Despite much experimental work, there is still a significant …

Of all the types of enzyme-catalyzed reactions, hydrolytic transformations involving amide
and ester bonds are the easiest to perform using proteases, esterases, or lipases. The key …

We have extended our investigations of the carbonic anhydrase (CA) cycle with the model
system [(H3N) 3ZnOH]+ and CO2 by studying further heterocumulenes and catalysts. We …

The catalytic mechanism of carboxypeptidase A (CPA) for the hydrolysis of ester substrates
is investigated using hybrid quantum mechanical/molecular mechanical (QM/MM) methods …

Carboxypeptidase is a Zn-dependent protease that specifically recognises and hydrolyses
peptides with a hydrophobic side chain at the C-terminal residue. According to hydrolysis …

Zinc metalloenzymes play a major role in key biological processes and carboxypeptidase‐A
(CPA) is a major prototype of such enzymes. The present work quantifies the energetics of …

Metallo-enzymes play an indispensible role in many biological functions, and their modes of
substrate binding and catalysis differ considerably from those of metal-free enzymes. A …