FIGURE 1.

Mtb ClpP1P2 cleaves peptide-amc substrates mainly after Leu, Phe, Ala, and especially Met. A, to determine cleavage preferences for the X₁ position, ClpP1P2 activity was measured continuously using Ac-X₃X₂X₁-amc fluorogenic peptides library (at 10 μm) in buffer A containing 30 nm ClpP1P2. The ClpP1P2 activity against the best substrates with a given amino acid in X₁ position is reflected in the graph. B, average rate of hydrolysis of substrates with a given amino acid in the X₁ position. The activity was measured as in Fig. A. RFU, relative fluorescence units.