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
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...
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-...
Optimal temperature and pH values were determined for both proteins using L-alanine- p -nitroanilide hydrochloride as a substrate for N-acetylmuramoyl-L-alanine amidase activity. Both proteins showed similar maximum activity values for pH (8) and temperature (50掳C). Furthermore, in silico ...
The sequence analysis showed 67% of identity with a N-acetylmuramoyl-l-alanine amidase protein with five non-identical LysM domains. The purified protein showed an optimal pH of 8.0 and heat resistance at 80 掳C for 10 min. L. sakei strain displayed antibacterial act...
Application of the method to the autolysin-endowed strain and an autolysis-deficient flaD-bearing mutant has revealed (i) that the N-acetylmuramoyl-l-alanine amidase behaves like an endoenzyme with an apparent Kcat(s−1) of 40, and (ii) that the residual enzyme activity in the flaD ...
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 ...
A purified preparation of N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28), a murein hydrolase from Escherichia coli, was found to lose its activity during incubation in the presence of bacterial phospholipid suspensions. Whether it was co-dispersed with the phospholipids or added to sonicated ...
The EDTA-treated CwlV1 did not have amidase activity. The amidase activity of the EDTA-treated CwlV1 was restored by the addition of Zn, Mn, and Cobut not by the addition of Mgand Ca. These results suggest that the amidases in the CwlB family are zinc amidases containing two glutamic ...
Analysis of the degradation products obtained by digestion of pneumococcal cell walls with Skl revealed that this enzyme is an N-acetylmuramoyl- l-alanine amidase (EC 3.5.1.28), showing optimum activity at 30 掳C and at a pH of 6.5. Skl is a unique member of the choline-binding family of...