Bacillus subtilis Lyt+ and Lyt- strains secrete peptidoglycan hydrolases.
The phenotypes characteristic of the pleiotropic lytic-deficient Bacillus subtilis mutants have been attributed to reductions in N-acetyl-muramoyl-L-alanine amidase (EC 3.5.1.28) and endo-beta-N-acetyl-glucosaminidase (EC 3.2.1.30). It is reported here that these peptidoglycan hydrolases are secreted. The FJ3 (lyt-1), FJ6 (lyt-2), and Ni15 (lyt-15) mutants secreted the enzymes in amounts comparable to a Lyt+ strain. Thus, the Lyt- mutants appear not be as deficient in the enzymes' synthesis as their cell-bound activities indicated. Based on the levels of cell-bound and extracellular activities measured during growth, it is suggested that the Lyt- phenotype may be due to a deficiency of the enzymes' acceptor(s) in cell walls.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism*; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D006596:Hexosaminidases / Q000378:metabolism*; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism; D010641:Phenotype
D010457:Peptidoglycan; D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase