Table 2.
Substrate specificity of three prolidases from P. horikoshii and P. furiosus.
| Substrates | Relative activity (%) | ||
|---|---|---|---|
| Phdpd | Zn-Phdpd | Zn-Pfprol(f) | |
| Met-Pro.HCl(a) | 100 | 100 | 100 |
| Val-Pro.HCl(a) | 53 | 4 | 10 |
| Ala-Pro.HCl(a) | 35 | 7 | 17 |
| Glu-Pro.HCl(a) | 28 | 5 | (e) |
| Phe-Pro.HCl(a) | 24 | 10 | 24 |
| Lys-Pro.HCl(a) | 17 | 0 | 10 |
| Gly-Pro.HCl(a) | 2 | (e) | 1 |
| Met-MCA.TosOH(b) | <0.1 | (e) | (e) |
| FRETS-25Xaa(c) | 0(d) | (e) | (e) |
(a)The specific activity in the presence of 1.2 mM CoCl2 is expressed as a percentage of the activity compared to that obtained with Met-Pro. The average values of three experiments are listed.
(b) V max was compared to that obtained with Val-Pro.
(c)FRETS is a fluorescence resonance energy transfer substrate library for determining endopeptidase specificity (Peptide Institute, Inc.).
(d)The endopeptidase activity was not detectable.
(d) Not examined.
(e) Reported results [13].