N-terminal methionine excision (NME) is the major proteolytic pathway responsible for the
diversity of N-terminal amino acids in proteins. Dedicated NME components have been …

At least one-third of enzymes contain metal ions as cofactors necessary for a diverse range
of catalytic activities. In the case of polymetallic enzymes (ie, two or more metal ions involved …

Histone deacetylases play a key role in regulating transcription and other cellular processes
by catalyzing the hydrolysis of ε-acetyl-lysine residues. For this reason, inhibitors of histone …

Abstract Analysis of the expressed protein complement of cells requires knowledge of the
diversity of post‐translational modifications that can occur and which can be transient or …

Nascent proteins emerging from translating ribosomes in bacteria are screened by a number
of ribosome-associated protein biogenesis factors, among them the chaperone trigger factor …

Determination of the crystal structure of human MetAP1 makes it possible, for the first time, to
compare the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from …

The structure of prolidase from the hyperthermophilic archaeon Pyrococcus furiosus (Pf prol)
has been solved and refined at 2.0 Å resolution. This is the first structure of a prolidase, ie, a …

The mammalian bradykinin-degrading enzyme aminopeptidase P (AP-P; EC 3.4. 11.9) is a
metal-dependent enzyme and is a member of the peptidase clan MG. AP-P exists as …

Prolidase is a ubiquitously distributed dipeptidase and the only dipeptidase in humans
capable of cleaving the peptide bond preceding the amino acids proline (Pro) or …

The nature of the interaction of the transition-state analogue inhibitor l-leucinephosphonic
acid (LPA) with the leucine aminopeptidase from Aeromonas proteolytica (AAP) was …