Protein Family Models

This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. This reference shows that the amino terminal region of Swiss:P14892 is required for bacteriolytic activity. [1]. 3070348. Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli. Potvin C, Leclerc D, Tremblay G, Asselin A, Bellemare G;. Mol Gen Genet 1988;214:241-248. [2]. 1677905. Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Wang X, Wilkinson BJ, Jayaswal RK;. Gene 1991;102:105-109. [3]. 8171031. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Cheng X, Zhang X, Pflugrath JW, Studier FW;. Proc Natl Acad Sci U S A 1994;91:4034-4038. (from Pfam)

Date:

2024-10-16

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides

Date:

2024-12-16