Pyroglutamate aminopeptidase I, also known as PGPase I, is an enzyme that catalyzes the hydrolysis of N-terminal pyroglutamic acid residues from peptides and proteins. This enzyme plays a significant role in protein metabolism and is involved in various biological processes, including the regulation of peptide hormone activity and the degradation of neuropeptides. Pyroglutamate aminopeptidase I is characterized by its specificity for substrates with a pyroglutamate residue at the N-terminus, which distinguishes it from other aminopeptidases. The enzyme is typically found in various tissues and can be influenced by factors such as pH and temperature, which affect its activity and stability. Its biochemical properties make it a subject of interest in research related to protein processing and potential therapeutic applications. Additionally, the enzyme's activity can be modulated by inhibitors, which can provide insights into its function and regulation within biological systems.

Pyroglutamate aminopeptidase I

9075-21-2: Pyroglutamate aminopeptidase I, also known as PGPase I, is an enzyme that catalyzes the hydrolysis of N-terminal pyroglutamic acid residues from peptides and proteins. This enzyme plays a significant role in protein metabolism and is involved in various biological processes, including the regulation of peptide hormone activity and the degradation of neuropeptides. Pyroglutamate aminopeptidase I is characterized by its specificity for substrates with a pyroglutamate residue at the N-terminus, which distinguishes it from other aminopeptidases. The enzyme is typically found in various tissues and can be influenced by factors such as pH and temperature, which affect its activity and stability. Its biochemical properties make it a subject of interest in research related to protein processing and potential therapeutic applications. Additionally, the enzyme's activity can be modulated by inhibitors, which can provide insights into its function and regulation within biological systems.

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.

CAS 9075-21-2

Pyroglutamate aminopeptidase I

Pyroglutamate aminopeptidase from pyrococcus furiosus, recombinant from E. coli

Ref: 3D-JAA07521