Pyroglutamyl aminopeptidase

A novel concept of using bioadhesive polymers as enzyme inhibitors has been developed [97]. Included are derivatives of poly acrylic acid, polycarbophil, and car-bomer to protect therapeutically important proteins and peptides from proteolytic activity of enzymes, endopeptidases (trypsin and a-chymotrypsin), exopeptidases (carboxypeptidases A and B), and microsomal and cytosolic leucine aminopeptidase. However, cysteine protease (pyroglutamyl aminopeptidase) is not inhibited by polycarbophil and carbomer [97]. 

This enzyme [EC 3.4.19.3], a member of the C15 peptidase family, is also known as pyroglutamyl-peptidase 1,5-oxoprolyl-peptidase, pyrrolidone-carboxylate peptidase, and pyroglutamyl aminopeptidase. This hydrolase catalyzes the conversion of a 5-oxoprolyl-peptide to produce 5-oxoproline and a peptide. The enzyme will not act on the 5-oxoprolyl peptide if the adjacent amino acid is l-proline. Enzyme activity is inhibited by thiol-blocking reagents. 

TAGZyme kit/E. coli MK(HQ)6QJ,-Protein and various, other His tags optimized for this kit Dipeptidyl aminopeptidase 1 (DPP 1) alone or a combination of DPP 1, glutamine cyclotransferase (GCT) and pyroglutamyl aminopeptidase (PGAP) UNYZYME Laboratories, Horsholm... 

Proline iminopeptidase [L-Prolylpeptide hydrolase] (3.4.11.5) is produced. [Formerly EC3.4.1.4.] Pyroglutamyl aminopeptidase [L-Pyroglutamyl-peptide hydrolase, Pyrrolidone-carboxylate peptidase] (3.4.11.8) is produced. [Removes pyroglutamate from various penultimate amino acid residues except L-proline. Occurs in Pseudomonas, Bacillus subtilis, rat liver.]... 

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