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. 2001 Feb;67(2):673–679. doi: 10.1128/AEM.67.2.673-679.2001

TABLE 1.

Substrate specificity of PP for Cbz peptides, Cbz amino acids, peptides, Ac peptides, and Ac amino acidsa

Substrate Activity (μmol/min/mg of enzyme) Relative activity (%)
10 mM
 Cbz-F 55.9 47
 Cbz-G-F 119 100
 Cbz-G-G-F 0.571 0.48
    ↓
 Cbz-G 63.0 53
    ↓
 Cbz-R 0.014 0.01
 G-F 107b 90
 G-G-F 1.21b 1.0
 G-G-G-F 0.551b 0.46
 Ac-G-F 105a 88
 Ac-G-G-F 0.773b 0.65
 Ac-G-G-G-F 0.48b 0.40
 5 mM
 Ac-M 38.1 43
 Ac-Y 37.3 29
 Ac-F 24.9 27
 Ac-A 10.5 15
 Ac-W 1.99 2.7
 Ac-G 7.40 2.1
a

The hydrolytic reaction was carried out at 85°C in 50 mM phosphate buffer (pH 7.5) containing 5% DMF. The cleavage site for the substrate is shown by the arrow. 

b

The hydrolytic activity (release of F) was measured by HPLC.