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cwlM | Probable peptidoglycan hydrolase; Cell-wall hydrolase that hydrolyzes the amide bond between N- acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to lyse whole mycobacteria, release peptidoglycan from the cell wall of M.luteus and M.smegmatis, and cleave N-acetylmuramoyl-L-alanyl-D- isoglutamine, releasing free N-acetylmuramic acid and dipeptide. (406 aa) | ||||
Rv3717 | Conserved hypothetical protein; Cell-wall hydrolase that hydrolyzes the amide bond between N- acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus, B.subtilis and E.coli W3110), thereby showing that it is a cell-wall hydrolase with broad-spectrum activity. May have a role in peptidoglycan fragment recycling. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. (241 aa) | ||||
Rv2525c | Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4). (240 aa) |