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Information on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase
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3.5.1.28 N-acetylmuramoyl-L-alanine amidaseSpecify your search results
Word Map
- 3.5.1.28
- endolysins
- staphylococcus
- aureus
- autolysins
- streptococcus
- listeria
- pneumococcal
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bacteriolytic
- murein
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autolytic
-
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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylmuramoyl-alanine amidase
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acetylmuramyl-alanine amidase
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acetylmuramyl-L-alanine amidase
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AMI1
AmiA
AmiC
AmiC2
AmiE
AmpD
Autolysin
cell separation amidase
cell wall amidase
Cell wall hydrolase
CwlB protein
cwlC
EC 3.4.17.7
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formerly
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EC 3.4.19.10
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formerly
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endolysin
GC-AmiC
LysBPS13
lysostaphin
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activities: N-acetyl muramyl-L-alanine amidase, glycylglycine endopeptidase and endo-beta-N-acetyl glucosamidase
LytA
LytA-like N-acetylmuramoyl-L-alanine amidase
LytAB6
LytAHER
Lytic amidase
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LytN
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LytN harbors LysM and histidine-dependent amidohydrolase/peptidase domains, the latter of which functions as both an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine endopeptidase
MSMEG_6281
Mtb peptidoglycan amidase
Mucopeptide aminohydrolase
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murein hydrolase
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MurnAc-lAA
N-acetyl-muramoyl-L-alanine amidase
N-acetylmuramic acid L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase
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
N-acetylmuramylalanine amidase
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N-acylmuramyl-L-alanine amidase
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NAM-amidase
NAMLAA
Npun_F1846
ORFL3
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Peptidoglycan hydrolase
PG amidase
phage endolysin
RC0497
RS15875
Rv3717
Skl
T3 lysozyme
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T7 lysozyme
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additional information
Autolysin
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Cell wall hydrolase
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endolysin
Bacillus cereus phage BPS13
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LysBPS13
Bacillus cereus phage BPS13
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N-acetylmuramoyl-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase
activity of a bifunctional autolysin
N-acetylmuramyl-L-alanine amidase
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N-acetylmuramyl-L-alanine amidase
Bacillus cereus phage BPS13
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additional information
the enzyme belongs to the peptidoglycan recognition protein, PGRP, family
additional information
the enzyme belongs to the peptidoglycan recognition protein, PGRP, family
additional information
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the enzyme is a member of the choline-binding family, subfamily CHAP-containing enzymes, of proteins
additional information
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the enzyme is a member of the choline-binding family, subfamily CHAP-containing enzymes, of proteins
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
catalytic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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PATHWAY SOURCE
PATHWAYS
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,
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SYSTEMATIC NAME
IUBMB Comments
peptidoglycan amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9013-25-6
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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
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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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?
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
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?
1,6-anhydromuropeptide + H2O
?
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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
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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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?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
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?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
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?
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
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?
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
?
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?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
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?
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
?
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?
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
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?
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
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?
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
?
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?
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
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?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
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?
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)
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?
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala + H2O
?
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?
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
?
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also murein extracted from cells grown in the presence of penicillin, N-acetylated murein
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?
MurNAc-L-Ala-D-isoGln-L-Lys + H2O
MurNAc + L-Ala-D-isoGln-L-Lys
MurNAc-tripeptide, minimum peptidoglycan fragment hydrolyzed by PGRP-L
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?
MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala + H2O
MurNAc + L-Ala-D-isoGln-L-Lys-D-Ala
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?
N-(beta-1,4-N-acetylglucosaminyl-N-acetylmuramoyl-L-alanyl-gamma-D-isoglutaminyl)-L-lysyl-D-alanine + H2O
?
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?
N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-tripeptide + H2O
?
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?
N-acetylmuramoyl-L-alanine-gamma-D-glutamyl-mesodiaminopimelic acid + H2O
?
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?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
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?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
?
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?
N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid + H2O
?
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?
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
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?
phospho-N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
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?
uridine diphospho-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid + H2O
?
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?
cell walls
?
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from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
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?
cell walls
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from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
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?
cell walls
?
Dubowvirus dv11
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cell wall anchor structures from staphylococcal surface proteins
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?
cell walls
?
Pneumococcal bacteriophage HB-3
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pneumococcal cell walls, labeled with [methyl-3H]choline, L-[4,5-3H]lysine monohydrochloride, or [2-14C]ethanolamine
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?
cell walls
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pneumococcal cell walls labeled with [methyl-3H] or [3H]lysine
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?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
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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
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?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
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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
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?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
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small synthetic peptidoglycan fragment
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?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
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small synthetic peptidoglycan fragment
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?
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
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?
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
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-
-
?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
-
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?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
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?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Bacillus cereus phage BPS13
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?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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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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?
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
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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, 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
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-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme hydrolyzes bacterial peptidoglycan
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?
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
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-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
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-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
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-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
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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
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-
?
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
?
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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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-
?
peptidoglycan + H2O
?
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the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
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-
?
peptidoglycan + H2O
?
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the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
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?
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
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-
ir
additional information
?
-
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
?
-
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