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
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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
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teichoic
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lysostaphin
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transglycosylase
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histidine-dependent
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n-acetylmuramidase
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choline-containing
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bacteriophage-encoded
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diaminopimelic
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muramidase
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siphoviridae
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phage-encoded
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n-acetylglucosaminidase
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endo-beta-n-acetylglucosaminidase
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lysodeikticus
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drug development
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agriculture
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diagnostics
- 3.5.1.28
- endolysins
- staphylococcus
- aureus
- autolysins
- streptococcus
- listeria
- pneumococcal
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bacteriolytic
- murein
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autolytic
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holins
- prophage
- muropeptides
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pgrps
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wall-binding
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teichoic
- lysostaphin
- transglycosylase
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histidine-dependent
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n-acetylmuramidase
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choline-containing
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bacteriophage-encoded
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diaminopimelic
- muramidase
- siphoviridae
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phage-encoded
- n-acetylglucosaminidase
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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
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results (Natural Substrates Products
Natural Substrates Products on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase
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NATURAL SUBSTRATE 
NATURAL 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
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?
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
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?
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
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the substrate is likely not turned over in vitro by AmpD
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?
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
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peptidoglucan + H2O
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cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor
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peptidoglycan + H2O
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enzyme is required for the recognition of peptidoglycan, a component of bacterial cell walls, and therefore critical for the immune response
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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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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
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additional information
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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
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?
additional information
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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
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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
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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
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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
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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
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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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determination of the sites of Bacillus thuringiensis cell wall cleavage by the enzyme, overview
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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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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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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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AmpD is involved in both peptidoglycan recycling and beta-lactamase induction
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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 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 performs cell wall lysis and is important in cell separation of Staphylococcus aureus
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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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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 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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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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