Fig. 3
Binding and kinetics of substrates and recognition tail truncations. a ITC binding curves for the 25mer peptide (obtained with the S577A mutant) and the 17 amino-acid recognition (linker and tail) sequence. b K d values of peptides examined by ITC shows the 35mer and 25mer bind with similar affinity, the leader does not bind, the tail on its own binds weakly and the contributes to binding energy. The peptides are colored as Fig. 1c with N-terminus at top. Error bars are standard error of the mean from the average of at least two independent measurements (Supplementary Table 3). c Michaelis–Menten curves show both the 13mer and 14mer are substrates for the enzyme. Fitted values for K d, K m, and k cat are shown in Supplementary Tables 2 and 3. Error bars are standard error of the mean from duplicate measurements. d Cyclic peptide produced after 1 h reaction with 1 μM GmPOPB and 200 μM of various peptide substrates. e Peptide produced after 16 h of reaction with 1 μM GmPOPB and 200 μM of various peptide substrates. Peptide sequences are colored as Fig. 1b and detailed in Supplementary Fig. 1
