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This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L-alanine amidase, N-acetylmuramyl-L-alanine amidase, N-acylmuramyl-L-alanine amidase, acetylmuramoyl-alanine amidase, N-acetylmuramic acid L-alanine amidase, acetylmuramyl-alanine amidase, N-acetylmuramylalanine amidase, N-acetylmuramoyl-L-alanine amidase type I, and N-acetylmuramoyl-L-alanine amidase type II. This enzyme participates in peptidoglycan biosynthesis. Autolysins and some phage lysins are examples of N-acetylmuramoyl-L-alanine amidases.
Campbell JN; Dierickx, L; Coyette, J; Leyh-Bouille, M; Guinand, M; Campbell, JN (1969). "An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-l-alanine amidase active on bacterial wall peptidoglycans". Biochemistry. 8 (1): 213–22. doi:10.1021/bi00829a031. PMID5777325.
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus