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4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
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?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
GlcNAc-beta-1,4-GlcNAc + H2O
?
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no deacetylation of the reducing GlcNAc residue
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
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deacetylates all GlcNAc residues of the oligomer except the reducing end ones
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN-beta-1,4-GlcNAc + acetate
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
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GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc is the favorable substrate. Deacetylates all GlcNAc residues of the oligomer except the reducing end ones
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN-beta-1,4-GlcNAc + acetate
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
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deacetylates all GlcNAc residues of the oligomer except the reducing end ones
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
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deacetylates all GlcNAc residues of the oligomer except the reducing end ones
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?
GlcNAc-Mur[-L-Ala-D-Glu]-GlcNAc-MurNAcr[-L-Ala-D-Glu] + H2O
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc
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?
glycolchitin + H2O
?
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poor substrate
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?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N',N''-triacetylchitopentaose + N,N'-diacetylchitopentaose + N-acetylchitopentaose + acetate
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almost quantitative conversion to mono-, di- and tri-de-acetylated products
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?
peptidoglycan + H2O
?
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?
peptidoglycan from Streptococcus suis + H2O
deacetylated peptidoglycan + acetate
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?
peptidoglycan from wild-type Streptococcus pneumoniae + H2O
deacetylated peptidoglycan + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
additional information
?
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(GlcNAc)5 + H2O
?
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?
(GlcNAc)5 + H2O
?
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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enzymatic deacetylation of chemically acetylated vegetative peptidoglycan from Bacillus cereus by BC1960 and BC3618 results in increased resistance to lysozyme digestion
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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effective in deacetylating cell wall peptidoglycan from the Gram(+) Bacillus cereus and Bacillus subtilis and the Gram(-) Helicobacter pylori
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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N-deacetylation is a major modification of Listeria peptidoglycan. PG N-deacetylation could be a general mechanism used by bacteria to evade the host innate immune system
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
peptidoglycan GlcNAc deacetylase protects the Gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan GlcNAc residues
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?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
contribution of lysozyme and peptidoglycan modifications during colonization of the upper respiratory tract analyzed
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN-beta-1,4-GlcNAc + acetate
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deacetylation of the chitin oligomer at position 3
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?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN-beta-1,4-GlcNAc + acetate
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deacetylation of the chitin oligomer at position 3
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?
GlcNAc-Mur[-L-Ala-D-Glu]-GlcNAc-MurNAcr[-L-Ala-D-Glu] + H2O
?
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i.e. 4S2P, deacetylation
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?
GlcNAc-Mur[-L-Ala-D-Glu]-GlcNAc-MurNAcr[-L-Ala-D-Glu] + H2O
?
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i.e. 4S2P, deacetylation
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
Q81P72, Q81RR3
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
Q81P72, Q81RR3
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peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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substrates: peptidoglycans digested by DL-endopeptidase, or by LD-endopeptidase, or by L-alanine amidase, the latter is a very poor substrate. Purified recombinant and truncated enzyme, expressed in Escherichia coli, deacetylates Bacillus subtilis peptidoglycan and its polymer, (-GlcNAc-MurNAc[-L-Ala-D-Glu]-)n. The enzyme deacetylates N-acetylmuramic acid not N-acetyl-D-glucosamine from the polymer. The enzyme PdaC is a unique enzyme exhibiting two different deacetylase activities. The enzyme works as a MurNAc deacetylase toward glycan strands containing L-Ala-D-Glu
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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substrates: peptidoglycans digested by DL-endopeptidase, or by LD-endopeptidase, or by L-alanine amidase, the latter is a very poor substrate. Purified recombinant and truncated enzyme, expressed in Escherichia coli, deacetylates Bacillus subtilis peptidoglycan and its polymer, (-GlcNAc-MurNAc[-L-Ala-D-Glu]-)n. The enzyme deacetylates N-acetylmuramic acid not N-acetyl-D-glucosamine from the polymer. The enzyme PdaC is a unique enzyme exhibiting two different deacetylase activities. The enzyme works as a MurNAc deacetylase toward glycan strands containing L-Ala-D-Glu
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peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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Helicobacter pylori is highly resistant to lysozyme (up to 50 mg/ml), but the HP310 mutant is less resistant compared with the parent strain. The peptidoglycan deacetylation appears to confer lysozyme resistance to escape immunedetection
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
peptidoglycan consists of alternating N-acetylglucosamine and N-acetylmuramic acid residues connected by beta-1,4 bonds and cross-linked via short peptide bridges
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
peptidoglycan consists of alternating N-acetylglucosamine and N-acetylmuramic acid residues connected by beta-1,4 bonds and cross-linked via short peptide bridges
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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peptidoglycan N-deacetylation is an important modification of Listeria peptidoglycan, which allows this human pathogen to evade the innate immune system
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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N-acetylated murein after lysozyme digestion
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
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?
additional information
?
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no activity with N-acetyl-D-glucosamine
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?
additional information
?
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reaction of the deacetylase with (GlcNAc-MurNAc)3 is less than 1/100 of that with peptidoglycan, while the enzyme is inactive towards (GlcNAc-MurNAc), GlcNAc-MurNAc, and monomeric N-acetylglucosamine derivatives
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?
additional information
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the enzyme is inactive towards all peptidoglycan precursors
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?
additional information
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the enzyme is inactive towards all peptidoglycan precursors
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?
additional information
?
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the enzyme is inactive towards all peptidoglycan precursors
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?
additional information
?
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the enzyme is inactive towards all peptidoglycan precursors
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?
additional information
?
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PdaC acts as a GlcNAc deacetylase toward chitin oligomers and as a MurNAc deacetylase toward Bacillus subtilis peptidoglycan, activity toward MurNAc is higher than toward GlcNAc
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?
additional information
?
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the purified recombinant enzyme shows no nuclease activity with DNA
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?
additional information
?
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PdaC acts as a GlcNAc deacetylase toward chitin oligomers and as a MurNAc deacetylase toward Bacillus subtilis peptidoglycan, activity toward MurNAc is higher than toward GlcNAc
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?
additional information
?
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the purified recombinant enzyme shows no nuclease activity with DNA
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?
additional information
?
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no substrates: N-acetyl putrescine, N-acetyl spermidine, N-acetyl cadaverine, and N-acetyl dipeptides Ac-D-Ala-D-Ala-OH, Ac-D-Ala-D-Ala-OCH3, Ac-DAla-L-Ala-OH, Ac-D-Ala-L-Ala-OCH3
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?
additional information
?
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no substrates: N-acetyl putrescine, N-acetyl spermidine, N-acetyl cadaverine, and N-acetyl dipeptides Ac-D-Ala-D-Ala-OH, Ac-D-Ala-D-Ala-OCH3, Ac-DAla-L-Ala-OH, Ac-D-Ala-L-Ala-OCH3
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?
additional information
?
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N-acetylmuramic acid is not a substrate. With N-acetylglucosamine as substrate D-glucosamine is formed
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?
additional information
?
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enzyme is inactive against peptidoglycans from Staphylococcus aureus, Staphylococcus carnosus or Escherichia coli. No substrate: N-acetylglucosamine
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?