3.5.1.28: N-acetylmuramoyl-L-alanine amidase
This is an abbreviated version!
For detailed information about N-acetylmuramoyl-L-alanine amidase, go to the full flat file.
Word Map on EC 3.5.1.28
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3.5.1.28
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endolysins
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staphylococcus
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aureus
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autolysins
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streptococcus
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listeria
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pneumococcal
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bacteriolytic
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murein
-
autolytic
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holins
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prophage
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muropeptides
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pgrps
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wall-binding
-
teichoic
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lysostaphin
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transglycosylase
-
histidine-dependent
-
n-acetylmuramidase
-
choline-containing
-
bacteriophage-encoded
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diaminopimelic
-
muramidase
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siphoviridae
-
phage-encoded
-
n-acetylglucosaminidase
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endo-beta-n-acetylglucosaminidase
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lysodeikticus
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drug development
-
agriculture
-
diagnostics
- 3.5.1.28
- endolysins
- staphylococcus
- aureus
- autolysins
- streptococcus
- listeria
- pneumococcal
-
bacteriolytic
- murein
-
autolytic
-
holins
- prophage
- muropeptides
-
pgrps
-
wall-binding
-
teichoic
- lysostaphin
- transglycosylase
-
histidine-dependent
-
n-acetylmuramidase
-
choline-containing
-
bacteriophage-encoded
-
diaminopimelic
- muramidase
- siphoviridae
-
phage-encoded
- n-acetylglucosaminidase
-
endo-beta-n-acetylglucosaminidase
- lysodeikticus
- drug development
- agriculture
- diagnostics
Reaction
Synonyms
1,6-anhydro-N-acetylmuramic acid-L-alanine amidase, 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, acetylmuramoyl-alanine amidase, acetylmuramyl-alanine amidase, acetylmuramyl-L-alanine amidase, AMI1, AmiA, AmiB, AmiC, AmiC2, AmiD, amidase 3, amidase-hydrolase, AmiE, AmpD, anhydroMurNAc-L-Ala amidase, AtlE, Autolysin, autolysin E, bacteriophage phiGVE2 amidase, cell separation amidase, cell wall amidase, Cell wall hydrolase, CwhA, CwlB protein, cwlC, CwlJ1, EC 3.4.17.7, EC 3.4.19.10, endolysin, GC-AmiC, GRCS_0011, LysBPS13, lysostaphin, LysSA97, LytA, LytA-like N-acetylmuramoyl-L-alanine amidase, LytAB6, LytAHER, Lytic amidase, Lytmu1/6, LytN, More, MSMEG_6281, Mtb peptidoglycan amidase, Mucopeptide aminohydrolase, murein hydrolase, MurnAc-lAA, Nacetylmuramoyl-L-alanine amidase activity, N-acetyl muramyl-L-alanine amidase, N-acetyl-muramoyl-L-alanine amidase, N-acetylmuramic acid L-alanine amidase, N-acetylmuramoyl-L-alanine amidase, N-acetylmuramoyl-l-alanine amidase B, N-acetylmuramoyl-L-alanine amidase type I, N-acetylmuramoyl-L-alanine amidase type II, N-acetylmuramyl-L-alanine amidase, N-acetylmuramylalanine amidase, N-acylmuramyl-L-alanine amidase, NAM-amidase, NAMLA amidase, NAMLAA, Npun_F1846, ORFL3, peptidoglycan amidase, peptidoglycan aminohydrolase, Peptidoglycan hydrolase, peptidoglycan recognition protein 2, peptidoglycan recognition protein SC1a, peptidoglycan recognition protein-L, PG amidase, PGLYRP2, PGRP, PGRP-L, PGRP-S4, PGRP-SB1, phage endolysin, phi26F_gp22, phiCP26F endolysin, phiGVE2 endolysin, PlyCP26F, PlyCP39O, PlyCpAmi, PlyGRCS, PlyPl23, RC0497, RS15875, Rv3717, SA97_036, short peptidoglycan recognition protein 4, Skl, Sle1, SleC, spore cortex lytic enzyme, T3 lysozyme, T7 lysozyme
ECTree
3.5.1.28 N-acetylmuramoyl-L-alanine amidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP
-
-
-
-
?
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
-
-
-
-
?
1,6-anhydro-N-acetylmuramic-acid-L-Ala-gamma-D-Glu-L-Lys + H2O
1,6-anhydro-N-acetylmuramate + L-Ala-gamma-D-Glu-L-Lys
-
-
-
?
1,6-anhydromuropeptide + H2O
?
-
AmpD has a strict specificity for 1,6-anhydromuropeptides, three-dimensional structure, active site structure, catalytic mechanism, Lys-162 and Tyr-63 are probably involved in substrate binding
-
-
?
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
?
-
the substrate is likely not turned over in vitro by AmpD
-
-
?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-Ala-D-isoglutaminyl-(L)-(beta-N-acetyl-glucosaminyl-(1-4)-N-acetylmuramoyl-L-Ala-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-Ala)-(D)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-(beta-N-acetyl-glucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine)-(D)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-(beta-N-acetyl-glucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine)-(D)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
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-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramic acid + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
-
-
-
?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
-
-
-
?
GlcNAc-anhydroMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
GlcNAc-anhydroMurNAc + L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala
biphasic behavior: rapid exponential phase preceding a linear phase (0.027 mM substrate, 0.000106 mM enzyme)
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala + H2O
?
-
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala + H2O
N-acetylglucosaminyl-N-acetylmuramic acid + L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
murein + H2O
?
-
also murein extracted from cells grown in the presence of penicillin, N-acetylated murein
-
-
?
MurNAc-L-Ala-D-isoGln-L-Lys + H2O
MurNAc + L-Ala-D-isoGln-L-Lys
MurNAc-tripeptide, minimum peptidoglycan fragment hydrolyzed by PGRP-L
-
-
?
MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala + H2O
MurNAc + L-Ala-D-isoGln-L-Lys-D-Ala
-
-
-
?
N-(beta-1,4-N-acetylglucosaminyl-N-acetylmuramoyl-L-alanyl-gamma-D-isoglutaminyl)-L-lysyl-D-alanine + H2O
?
-
-
-
-
?
N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-tripeptide + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanine-gamma-D-glutamyl-mesodiaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
phospho-N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
uridine diphospho-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
cell walls
?
-
from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
-
-
?
cell walls
?
-
from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
-
-
?
cell walls
?
Dubowvirus dv11
-
cell wall anchor structures from staphylococcal surface proteins
-
-
?
cell walls
?
Pneumococcal bacteriophage HB-3
-
pneumococcal cell walls, labeled with [methyl-3H]choline, L-[4,5-3H]lysine monohydrochloride, or [2-14C]ethanolamine
-
-
?
cell walls
?
-
pneumococcal cell walls labeled with [methyl-3H] or [3H]lysine
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
-
the cell separation amidase can utilize the small synthetic peptidoglycan a pentapeptide fragment as substrate. AmiC can cleave one peptide stem from synthetic PG dimer
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
-
the cell separation amidase can utilize the small synthetic peptidoglycan a pentapeptide fragment as substrate. AmiC can cleave one peptide stem from synthetic PG dimer
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
-
small synthetic peptidoglycan fragment
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
-
small synthetic peptidoglycan fragment
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala + H2O
N-acetylglucosaminyl-N-acetylmuramic acid + L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala + H2O
N-acetylglucosaminyl-N-acetylmuramic acid + L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
-
-
-
?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
-
-
-
?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Bacillus cereus phage BPS13
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, the immunostimulatory properties of PGRP-SC1B-degraded peptidoglycan are highly reduced
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, peptidoglycan substrate from Escherichia coli, PGRP-SB1 is highly active against peptidoglycans that have a diaminopimelic acid residue in the cross-linking peptide, but lacks activity to most lysine-containing peptidoglycans
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, peptidoglycan substrates from Staphylococcus aureus, Micrococcus luteus, and Bacillus megaterium, the enzyme hydrolyzes the lactylamide bond between the glycan strand and the cross-linking peptides, analysis of the cleavage products by mass spectrometry
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme hydrolyzes bacterial peptidoglycan
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
the enzyme performs cell wall lysis by cleavage of N-acetylmuramyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diamino [3,4,5-3H]pimelic acid (3H-MTP)
-
-
?
peptidoglucan + H2O
?
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
-
-
?
peptidoglucan + H2O
?
PGRP-L hydrolyzes the amide bond between MurNAc and L-Ala of peptidoglycan, Cys-419 is required for the amidase activity, polymeric soluble uncross-linked peptidoglycan from Staphylococcus aureus, digest products
-
-
?
peptidoglucan + H2O
?
cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor
-
-
?
peptidoglucan + H2O
?
LytA structure, 36.6 kDa modular enzyme comprising an N-terminal catalytic domain plus the C-terminal choline-binding domain, the former catalyzes the hydrolysis of the N-acetylmuramoyl-L-alanine bond present in the pneumococcal peptidoglycan backbone, fundamental role of the 11 C-terminal residues in the catalytic activity of LytA
-
-
?
peptidoglycan + H2O
?
-
enzyme is required for the recognition of peptidoglycan, a component of bacterial cell walls, and therefore critical for the immune response
-
-
?
peptidoglycan + H2O
?
-
the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
-
-
?
peptidoglycan + H2O
?
-
the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
-
-
?
peptidoglycan + H2O
peptidoglycan-derived fragment peptides
-
enzyme AmiC displays high basal activity on peptidoglycan. In vivo assay of HA-tagged recombinant enzyme in Escherichia coli cells, usage of fluorescein-labeled peptidoglycan. Digesting gonococcal PG with AmiC results in the recovery of soluble fragments of predicted masses matching tripeptide stem (L-Ala-gamma-D-Glu-mDAP), tetrapeptide stem (L-Ala-gamma-D-Glu-mDAP-D-Ala), pentapeptide stem (L-Ala-gamma-D-Glu-mDAPD-Ala-D-Ala), cross-linked tetrapeptide-tripeptide (4-3), crosslinked tetrapeptide-tetrapeptide (4-4), and cross-linked tetrapeptide-tetrapeptide-tetrapeptide (4-4-4). Substrate specificity of wild-type and mutant enzymes and product release analysis, detailed overview
-
-
ir
peptidoglycan + H2O
peptidoglycan-derived fragment peptides
-
enzyme AmiC displays high basal activity on peptidoglycan. In vivo assay of HA-tagged recombinant enzyme in Escherichia coli cells, usage of fluorescein-labeled peptidoglycan. Digesting gonococcal PG with AmiC results in the recovery of soluble fragments of predicted masses matching tripeptide stem (L-Ala-gamma-D-Glu-mDAP), tetrapeptide stem (L-Ala-gamma-D-Glu-mDAP-D-Ala), pentapeptide stem (L-Ala-gamma-D-Glu-mDAPD-Ala-D-Ala), cross-linked tetrapeptide-tripeptide (4-3), crosslinked tetrapeptide-tetrapeptide (4-4), and cross-linked tetrapeptide-tetrapeptide-tetrapeptide (4-4-4). Substrate specificity of wild-type and mutant enzymes and product release analysis, detailed overview
-
-
ir
additional information
?
-
bacteriolytic/cell wall hydrolytic amidase
-
-
?
additional information
?
-
-
bacteriolytic/cell wall hydrolytic amidase
-
-
?
additional information
?
-
A0A1J9W3F9
recombinant enzyme CwlJ1 shows activity against the spore cortical fragments of Bacillus anthracis when added exogenously. CwlJ1 is active on both decoated spores and spore cortical fragments. The Bacillus spore cortex is composed of a thick layer of peptidoglycan (PG) containing alternating beta-1,4 linked N-acetylglucosamine (NAG), N-acetylmuramic acid (NAM), and muramic acid-delta-lactam (MAL) residues, with NAM residues attached to either tetrapeptide (TP) or a single L-Ala residue
-
-
?
additional information
?
-
-
recombinant enzyme CwlJ1 shows activity against the spore cortical fragments of Bacillus anthracis when added exogenously. CwlJ1 is active on both decoated spores and spore cortical fragments. The Bacillus spore cortex is composed of a thick layer of peptidoglycan (PG) containing alternating beta-1,4 linked N-acetylglucosamine (NAG), N-acetylmuramic acid (NAM), and muramic acid-delta-lactam (MAL) residues, with NAM residues attached to either tetrapeptide (TP) or a single L-Ala residue
-
-
?
additional information
?
-
A0A1J9W3F9
CwlJ1 mainly recognizes large segments of glycan chains in the cortex instead of the minimal structural unit tetrasaccharide, with specificity for muramic acid-delta-lactam-containing glycan chains and preference for the tetrapeptide side chain. The enzyme cleaves Bacillus anthracis spore cortex peptidoglycan, structure, and specificity of CwlJ1 on spore core fragements, overview. Mass spectrometry analysis of muropeptides released from digested spore cortical fragments
-
-
?
additional information
?
-
-
CwlJ1 mainly recognizes large segments of glycan chains in the cortex instead of the minimal structural unit tetrasaccharide, with specificity for muramic acid-delta-lactam-containing glycan chains and preference for the tetrapeptide side chain. The enzyme cleaves Bacillus anthracis spore cortex peptidoglycan, structure, and specificity of CwlJ1 on spore core fragements, overview. Mass spectrometry analysis of muropeptides released from digested spore cortical fragments
-
-
?
additional information
?
-
the enzyme shows very high lytic activity against Bacillus anthracis strain Sterne and Bacillus thuringiensis strain 97-27 isolates. More than 90% of the Bacillus anthracis cells are lysed by 1 nM protein and 99% are lysed by 50 nM protein in 60 min. Exposure to 10 nM for 10 min results in significantly less than 1% survival
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-
?
additional information
?
-
the enzyme shows very high lytic activity against Bacillus anthracis strain Sterne and Bacillus thuringiensis strain 97-27 isolates. More than 90% of the Bacillus anthracis cells are lysed by 1 nM protein and 99% are lysed by 50 nM protein in 60 min. Exposure to 10 nM for 10 min results in significantly less than 1% survival
-
-
?
additional information
?
-
-
the enzyme shows very high lytic activity against Bacillus anthracis strain Sterne and Bacillus thuringiensis strain 97-27 isolates. More than 90% of the Bacillus anthracis cells are lysed by 1 nM protein and 99% are lysed by 50 nM protein in 60 min. Exposure to 10 nM for 10 min results in significantly less than 1% survival
-
-
?
additional information
?
-
-
AmiE hydrolyzes the N-acetylmuramoyl-L-Ala bond of N-acetylmuramic acid peptides releasing N-acetylglucosamine, N-acetylmuramic acid, and peptides, but does not hydrolyze this bond of muropeptides containing N-acetylglucosamine at the nonreducing end
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-
?
additional information
?
-
-
AmiE hydrolyzes the N-acetylmuramoyl-L-Ala bond of N-acetylmuramic acid peptides releasing N-acetylglucosamine, N-acetylmuramic acid, and peptides, but does not hydrolyze this bond of muropeptides containing N-acetylglucosamine at the nonreducing end
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-
?
additional information
?
-
-
determination of the sites of Bacillus thuringiensis cell wall cleavage by the enzyme, overview
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-
?
additional information
?
-
-
the recombinant enzyme shows cell wall binding ability and amidase activity in vitro
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-
?
additional information
?
-
-
recombinant His-tagged CwlC proteins purified from Escherichia coli were able to directly bind to and digest the Bacillus thuringiensis cell wall
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-
?
additional information
?
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recombinant His-tagged CwlC proteins purified from Escherichia coli were able to directly bind to and digest the Bacillus thuringiensis cell wall
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additional information
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determination of the sites of Bacillus thuringiensis cell wall cleavage by the enzyme, overview
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additional information
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the recombinant enzyme shows cell wall binding ability and amidase activity in vitro
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additional information
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the enzyme hydrolyses an Escherichia coli peptidoglycan
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additional information
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in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC
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additional information
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enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan
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additional information
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in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC
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additional information
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enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan
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additional information
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in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC
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additional information
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enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan
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additional information
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AmpD is involved in both peptidoglycan recycling and beta-lactamase induction
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additional information
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not: L-Ala-p-nitroanilide, D-Ala-p-nitroanilide, Gly-p-nitroanilide
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additional information
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the recombinant enzyme shows lytic activity against Clostridium perfringens cells
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additional information
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the enzyme performs cell wall lysis, and shows antibacterial activity against Bacillus megaterium
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additional information
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the enzyme does not show antibacterial activity
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additional information
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the enzyme has no activity on MurNAc-L-Ala-D-Glu
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additional information
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the enzyme has no activity on MurNAc-L-Ala-D-Glu
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additional information
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PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
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additional information
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PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
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additional information
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no activity on polymerized peptidoglycan
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additional information
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no activity on polymerized peptidoglycan
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additional information
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no activity on polymerized peptidoglycan
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additional information
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the enzyme performs cell wall lysis as peptidoglycan-degrading amidase, but can also promote autolysis in Neisseria gonorrhoeae, other enzymes are also involved in autolysis
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additional information
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enzyme AmiC displays high basal activity on peptidoglycan. Gonococcal AmiC (GC-AmiC) activity on whole GC sacculi, solubilization of whole gonococcal sacculi
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additional information
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enzyme AmiC displays high basal activity on peptidoglycan. Gonococcal AmiC (GC-AmiC) activity on whole GC sacculi, solubilization of whole gonococcal sacculi
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additional information
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the enzyme cleaves the amide linkage between the stem peptides and the lactyl moiety of muramoyl residues in bacterial cell wall heteropolymer peptidoglycan
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additional information
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the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide
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additional information
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the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide
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additional information
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the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide
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additional information
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the enzyme performs cell wall lysis and is important in cell separation of Staphylococcus aureus
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additional information
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the activity of recombinant C-terminal and N-terminal enzyme fragments towards cell wall peptidoglycans is analyzed by MALDI-TOF MS
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additional information
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AtlE is involved in the initial attachment of the cells to polymer surfaces and thus in biofilm formation
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additional information
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AtlE is a multifunctional, surface-associated protein having both enzymic, 60 kDa amidase and 52 kDa glucosaminidase, and adhesive functions, AtlE binds to vitronectin
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additional information
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cell walls are treated with enzyme PlyGRCS, revealing that the catalytic activity is an amidase or endopeptidase, PlyGRCS spectrum of lytic activity, overview. The enzyme shows N-acetylmuramoyl-L-alanine amidase activity
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs lysis of pneumococcal, choline-containing cell walls
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs lysis of pneumococcal, choline-containing cell walls
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additional information
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N-acetylmuramoyl-L-alanine amidase LytA shows the greatest efficiency in disintegrating Streptococcus pneumoniae biofilms. Biofilms formed by Streptococcus pseudopneumoniae and Streptococcus oralis are not destroyed by the Streptococcus pneumoniae autolysin LytA
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additional information
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N-acetylmuramoyl-L-alanine amidase LytA shows the greatest efficiency in disintegrating Streptococcus pneumoniae biofilms. Biofilms formed by Streptococcus pseudopneumoniae and Streptococcus oralis are not destroyed by the Streptococcus pneumoniae autolysin LytA
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additional information
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N-acetylmuramoyl-L-alanine amidase activity is measured according to the protocol described previously. This method is based on the degradation of free muramic acid resulting from cleavage of the amide bond in the peptidoglycan to lactic acid followed by degradation of the latter to acetaldehyde which can be determined colorimetrically with 4-phenylphenol. Spectrophotometric measurements
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