Pfu Aminopeptidase I is a thermostable exo-type aminopeptidase isolated from Pyrococcus furiosus. It is produced as a recombinant protein, which liberates the N-terminal amino acid from proteins and peptides. This enzyme has a wide range of substrate specificity, and it does not hydrolyze peptide bonds at the α-amino residue side of proline (X-Pro). It is significantly activated in the presence of a Co2+ ion.

Applications

• Liberates the N-terminal amino acids up to X-Pro from proteins and peptides

Source

Recombinant Escherichia coli encoding the Pyrococcus furiosus aminopeptidase I gene

Properties

• Molecular weight: 37.483 kDa (calculated), 36–37 kDa (SDS-PAGE) 
• Isoelectric point: 4.6–4.65
• Inhibitor: EDTA (completely inhibited at 0.1 mM)
• Optimum pH: 5.5–8.0 (in the presence of 20 µM Co2+ at 90°C)
• Optimum temperature: 80°C (in the presence of 20 µM Co2+ and pH 6.0) 95°C (without Co2+ at pH 6.0) 
• Thermal stability: 65% activity after 4 hours at 90°C (without Co2+ at pH 8.0)

Definition of activity

One unit of enzyme activity corresponds to the amount required to hydrolyze 1 µmol of Leucine-p-nitroanilide at 75°C, pH 8.0 in one minute.

Activities

• >16 U/mg protein (without Co2+)
• >80 U/mg protein (in the presence of 20 µM Co2+)

Form

Lyophilized