Low et al, The Journal of Biological Chemistry.

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Structure and Lytic Activity of a Bacillus anthracis Prophage Endolysin Low et al, 2005. The Journal of Biological Chemistry. Protein: N-acetylmuramoyl-L-alanine amidase (PlyL), λ Ba02 endolysin Uniprot: Q81WA9 Evidence Code: IDA GO: 0009253, peptidoglycan catabolic process (biological process) GO: 0008745, N-acetylmuramoyl-L-alanine amidase activity (molecular function) Transfers: Hakuna, Megatron, Eyuki Petidoglycan subjected to PlyL; graph shows release of Alanine due to PlyL cleaving the amide bond between N-acetylmuramic acid and L-alanine

Comparison of crystal structure of PlyL with other endolysins. Bacillus Prophage Endolysin Structure Time course assay where (PlyL) lysed 4 different bacillus species cultures within 400 seconds. Figure A, full-length. Figure B, N-Terminal.