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. 2023 Aug 16;19(8):e1011563. doi: 10.1371/journal.ppat.1011563

Fig 4. Enzymatic activity of TvNlpC_B3 and TvNlpC_B5.

Fig 4

(A) The catalytic active and inactive versions of these enzymes, as indicated, were incubated with tetrapeptide-rich PG from E. coli MC1061Δ6LDT (left side) or pentapepide-rich PG from strain CS703-1 (right side). Muropepides were released by cellosyl, reduced with sodium borohydride and separated by HPLC. Peaks of the main cleavage products were numbered 1 to 3. (B) Proposed structures of the main muropeptides and their TvNlpC products. Black arrows indicate sites of efficient cleavage detected from both TvNlpC enzymes. Grey arrows indicate less efficient cleavage sites. G, N-acetylglucsoamine; M(r), N-acetylmuramitol; L-Ala, L-alanine; D-iGlu, D-isoglutamate; D-Glu, D-glutamate; m-Dap, meso-diaminopimelic acid; D-Ala, D-alanine.