CAS 9075-21-2: Pyroglutamate aminopeptidase I

Pyroglutamate aminopeptidase from Pyrococcus furiosus, recombinant from E. coli, is an enzymatic product that specifically targets N-terminal pyroglutamyl residues in peptide chains. This enzyme is derived from the hyperthermophilic archaeon Pyrococcus furiosus, which allows it to exhibit high thermal stability and activity across a broad range of temperatures. Being produced recombinantly in E. coli ensures consistent availability and purity suitable for scientific applications. The mode of action of this aminopeptidase involves the cleavage of pyroglutamyl residues from the N-terminus of peptides, facilitating subsequent analyses and modifications. This enzymatic activity is crucial because pyroglutamate formation can inhibit peptide processing and sequencing reactions, posing challenges in proteomics and protein characterization. Applications of Pyroglutamate aminopeptidase include its use in peptide sequencing workflows, where it enables or enhances the identification of protein and peptide structures by removing blocking pyroglutamyl groups. Its stability at high temperatures also makes it valuable in applications where heat-resistant enzymes are required, allowing for effective peptide modification under various experimental conditions.