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The taxonomic range for the selected organisms is: Achromobacter lyticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-acetylmuramoyl-l-alanine amidase, pglyrp2, cell wall hydrolase, t7 lysozyme, n-acetylmuramyl-l-alanine amidase, phage endolysin, namlaa, pgrp-l, cwlj1, amic2,
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CwhA
cell wall hydrolytic amidase
acetylmuramoyl-alanine amidase
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acetylmuramyl-alanine amidase
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acetylmuramyl-L-alanine amidase
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Cell wall hydrolase
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Mucopeptide aminohydrolase
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N-acetylmuramic acid L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase type I
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N-acetylmuramoyl-L-alanine amidase type II
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N-acetylmuramyl-L-alanine amidase
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N-acetylmuramylalanine amidase
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N-acylmuramyl-L-alanine amidase
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hydrolysis of peptide bond
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peptidoglycan amidohydrolase
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peptidoglucan + H2O
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ChwA primarily hydrolyzes the N-acetylmuramoyl-L-alanyl amide bond, splits the linkage between polysaccharides and peptides, bacteriolytic/cell wall hydrolytic amidase, CwhA lyses CHCl3-treated Escherichia coli JM109 most efficiently, followed by Micrococcus luteus, Staphylococcus aureus IFO 13276, Enterococcus faecalis IFO 3971, Pediococcus acidilactici IFO3385 and intact Escherichia coli JM109
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additional information
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additional information
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bacteriolytic/cell wall hydrolytic amidase
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additional information
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bacteriolytic/cell wall hydrolytic amidase
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additional information
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additional information
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bacteriolytic/cell wall hydrolytic amidase
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additional information
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bacteriolytic/cell wall hydrolytic amidase
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additional information
probably a metalloenzyme, no effect on lytic activity by Zn2+, Ca2+ or Mg2+, each at 5 mM
additional information
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probably a metalloenzyme, no effect on lytic activity by Zn2+, Ca2+ or Mg2+, each at 5 mM
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1,10-phenanthroline
strong, 5 mM, 94% inhibition
dithiothreitol
5 mM, 53% inhibition
EDTA
less inhibitory than 1,10-phenanthroline, 10 mM, 25% inhibition
NaCl
sensitive to salt concentration, loses its lytic activity in 10 mM Tris-HCl containing 100 mM NaCl
Tris-HCl
lytic activity in 30 mM Tris-HCl is only 30% of that in 10 mM solution, almost inactive in 70 mM Tris-HCl
additional information
not inhibited by diisopropylfluorophosphate, iodoacetic acid, Zn2+, Ca2+, Mg2+, each at 5 mM
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additional information
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not inhibited by diisopropylfluorophosphate, iodoacetic acid, Zn2+, Ca2+, Mg2+, each at 5 mM
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SwissProt
brenda
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CWHA_ACHLY
177
0
19395
Swiss-Prot
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19396
1 * 19396, sequence calculation
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monomer
1 * 19396, sequence calculation
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Li, S.; Norioka, S.; Sakiyama, F.
Purification, characterization, and primary structure of a novel cell wall hydrolytic amidase, CwhA, from Achromobacter lyticus
J. Biochem.
127
1033-1039
2000
Achromobacter lyticus (P81717), Achromobacter lyticus
brenda
3.5.1.28 N-acetylmuramoyl-L-alanine amidase
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The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
