A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence ... The Tn551 insertion site of the autolysis-deficient Staphylococcus aureus mutant RUSAL2 was cloned and used to identify the autolysis gene at...
The gene encoding N-acetylmuramoyl-L-alanine amidase in Latilactobacillus sakei isolated from a fermented meat product was cloned in two forms: its complete sequence (AmiC) and without one of its anchoring LysM domains (AmiLysM4). Deletion of the LysM domain is believed to affect the target ...
We identified a gene encoding the N-acetylmuramoyl-L-alanine amidase (amiB) of Vibrio anguillarum, which catalyzes the degradation of peptidoglycan in bacteria. The entire open reading frame (ORF) of the amiB gene was composed of 1,722 nucleotides and 573 amino acids. The deduced amino acid ...
This chapter describes the activity, specificity and structural chemistry of N-Acetylmuramoyl- l -alanine amidase. N-Acetylmuramoyl- l -alanine amidases are peptidoglycan hydrolases with the specificity to cleave the amide bond between the lactyl group of the muramic acid and the α-amino group of...
Skl, a novel choline-binding N- acetylmuramoyl-L-alanine amidase of Streptococcus mitis SK137 containing a CHAP domain. FEBS Lett. 580:1959-1964.Llull D, Lopez R & Garcia E (2006) Skl, a novel choline-binding N-acetylmuramoyl-L- alanine amidase of Streptococcus mitis SK137 containing a ...
Site-directed mutagenesis was performed on 20 highly conserved amino acid residues within the catalytic domain of CwlC. The amidase activity was lost completely on single amino acid substitutions at two residues (Glu-24 and Glu-141). Similarly, the substitution of the two glutamic acid residues ...