Pyroglutamate Aminopeptidase from Pyrococcus furiosus

Pyroglutamate Aminopeptidase from Pyrococcus furiosus, also called the deblocking aminopeptidase, is a 42 kDa protein and belongs to aminopeptidase A family. It shares sequence homology with aminopeptidase in the active site, with conserved zinc and cobalt binding residues.

Thermostable aminopeptidase that liberates N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation.

The enzyme from Sigma has been used for the removal of pyroglutamate (pGlu) N-terminal blocking group, under reduced conditions, prior to N-terminal sequencing of purified cassiicolin.

Pyroglutamate Aminopeptidase, from Pyrococcus furiosus is a recombinant, thermostable aminopeptidase that is expressed in Escherichia coli. It is used to cleave pyroglutamic acid which allows analysis of N-terminal sequences of peptides.

This enzyme is specific for N-terminal pyroglutamic acids. It cleaves the N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation. The optimal temperature range is 95 to 100 °C and the optimal pH range is 6.0 to 9.0.

Pyroglutamate Aminopeptidase (PGP 1) interacts with immunoglobulin, functions as inflammatory cytokine and modulates immune response. The levels PGP 1 is elevated during inflammation.

Lyophilized powder containing sodium phosphate

Reconstitute the vial of enzyme with 50 μl of 50 mM sodium phosphate, pH 7.0, with 10 mM DTT and 1 mM EDTA. The reconstituted solution should be stored at -20 °C.

One unit will hydrolyze 1 μmol of pyroglutamate p-nitroanilide per minute at pH 7.0 at 37 °C.