TABLE 3.
Substrate specificity of native and recombinant P. furiosus lysine aminopeptidase
| Substratea (with p-nitroanilide amino acids) | % Relative activityb for:
|
|
|---|---|---|
| n-KAP | r-KAP | |
| Lys-pNA | 100 | 100 |
| Arg-pNA | 34 | 47 |
| Leu-pNA | 0 | 7 |
| Pro-pNA | 0 | 6 |
| Ala-pNA | 0 | 3 |
| Gly-pNA | 4 | 0.7 |
| His-pNA | 5 | 0 |
| Phe-pNA | 14 | 0 |
| Ac-Phe-pNA | 4 | 0 |
a
All substrates were used at a final concentration of 10 mM.
b
The rate of hydrolysis is expressed as a percentage of the activity compared to that obtained by using Lys-pNA as the substrate at 100°C, where 100% activity corresponds to 1,900 and 2,200 U/mg for native and recombinant KAP, respectively.