Most amidases are able to act on intact cell wall peptidoglycan, either associated with living bacteria or as isolated peptidoglycan, resulting in a loss of absorbance by the insoluble substrate. A general assay for peptidoglycan hydrolases by zymogram activity has been developed. The assay for ...
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 l-al...
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 伪-amino group of l-...
PGRP-SB1 :an N-acetylmuramoyl L-alanine amidase with antibacterial activity[ J]. Biochem Biophys Res Commun,2006,350(4) :994 -999.Mellroth P, Steiner H. PGRP-SB1: an N-acetylmuramoyl l-alanine amidase with antibacterial activity. Biochem Biophys Res Comm. 2006; 350: 994-9....
The assay for amidase activity is the hydrolysis of peptidoglycan substrate followed by the identification of new l -alanine N-termini. The amidases show varying substrate specificities and biochemical properties. The LytA autolytic amidase of Streptococcus pneumoniae requires cell walls containing choline...
coli clone exhibited an N-acetylmuramoyl-L-alanine amidase activity. Insertional mutagenesis confirmed that the latter enzyme was associated with SPβ-phage-mediated ceil lysis. Analysis of the neighbouring sequence suggested that the two ORFs immediately downstream of blyA and belonging to the same ...
PGRP-SB1 is a peptidoglycan degrading enzyme with N-acetylmuramoyl l-alanine amidase activity and does thus belong to the same class as the previously characterised PGRP-SC1b, PGRP-LB, M.m. PGRP-L, and H.s.PGRP-L [4], [5], [6], [8]. These enzymes degrade peptidoglycan by hydrolys...
Antimicrobial activity of N-acetylmuramoyl-L-alanine amidase produced by Lactobacillus sakei, against Leuconostoc mesenteroides and Weissella viridescensdoi:10.1016/j.jbiotec.2019.05.275L.A. Lopez ArvizuI. Garcia CanoA. FarrEsE. Ponce Alquicira
These amino acids, although required, are not sufficient for the amidase activity, because changing them to the "active" configuration does not convert PGRP-S into an active amidase. In conclusion, human PGRP-L is an N -acetylmuramoyl- l -alanine amidase and this function is conserved in ...