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. 2017 May 5;292(26):10835–10844. doi: 10.1074/jbc.M117.783464

Figure 3.

Figure 3.

Minimal substrate for KW_cyclase. a, sequence alignment of ME_30 peptide homologs found in various bacteria. The putative peptide leader sequence is highlighted in black. The conserved residues are highlighted in blue, whereas the residues involved in the cyclic KGDGW peptide are highlighted in red. The second KGDGW motif, found in S. thermophilus is highlighted in purple. St, S. thermophilus; Sm, S. mitis; Sa, S. agalactiae; Ll, L. lactis; Pa, P. aeruginosa. b, sequences of the ME_30, MK_21, and VK_14 peptides. c, MALDI-TOF MS analysis of MK_21 (left panel) and VK_14 (right panel) peptides before (top traces) or after (bottom traces) incubation with KW_cyclase (see below for experimental conditions). d, kinetic analysis of the reaction catalyzed by KW_cyclase in the presence of the ME_30 peptide. The data represent the mean ± S.D. of three independent reactions. See below for experimental conditions. e, kinetic analysis of the reaction catalyzed by KW_cyclase in the presence of the MK_21 peptide. Reactions were performed by incubating the reconstituted KW_cyclase (68 μm) with peptide substrate (1 mm), SAM (1 mm), DTT (3 mm), and sodium dithionite (2 mm) under anaerobic conditions. The data represent the mean ± S.D. of three independent reactions.