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4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
GlcNAc-beta-1,4-GlcNAc + H2O
?
-
no deacetylation of the reducing GlcNAc residue
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
deacetylates all GlcNAc residues of the oligomer except the reducing end ones
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN-beta-1,4-GlcNAc + acetate
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
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
-
-
?
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
?
-
deacetylates all GlcNAc residues of the oligomer except the reducing end ones
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
deacetylates all GlcNAc residues of the oligomer except the reducing end ones
-
-
?
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
-
-
-
?
glycolchitin + H2O
?
-
poor substrate
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N',N''-triacetylchitopentaose + N,N'-diacetylchitopentaose + N-acetylchitopentaose + acetate
-
-
almost quantitative conversion to mono-, di- and tri-de-acetylated products
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan from Streptococcus suis + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
peptidoglycan from wild-type Streptococcus pneumoniae + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
additional information
?
-
(GlcNAc)5 + H2O
?
-
-
-
?
(GlcNAc)5 + H2O
?
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
enzymatic deacetylation of chemically acetylated vegetative peptidoglycan from Bacillus cereus by BC1960 and BC3618 results in increased resistance to lysozyme digestion
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
effective in deacetylating cell wall peptidoglycan from the Gram(+) Bacillus cereus and Bacillus subtilis and the Gram(-) Helicobacter pylori
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
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
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
peptidoglycan GlcNAc deacetylase protects the Gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan GlcNAc residues
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
contribution of lysozyme and peptidoglycan modifications during colonization of the upper respiratory tract analyzed
-
-
?
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
-
deacetylation of the chitin oligomer at position 3
-
-
?
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
-
deacetylation of the chitin oligomer at position 3
-
-
?
GlcNAc-Mur[-L-Ala-D-Glu]-GlcNAc-MurNAcr[-L-Ala-D-Glu] + H2O
?
-
i.e. 4S2P, deacetylation
-
-
?
GlcNAc-Mur[-L-Ala-D-Glu]-GlcNAc-MurNAcr[-L-Ala-D-Glu] + H2O
?
-
i.e. 4S2P, deacetylation
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
Q81P72, Q81RR3
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
Q81P72, Q81RR3
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
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
-
-
?
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
-
-
?
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
peptidoglycan N-deacetylation is an important modification of Listeria peptidoglycan, which allows this human pathogen to evade the innate immune system
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
N-acetylated murein after lysozyme digestion
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
additional information
?
-
-
no activity with N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme is inactive towards all peptidoglycan precursors
-
-
?
additional information
?
-
the enzyme is inactive towards all peptidoglycan precursors
-
-
?
additional information
?
-
the enzyme is inactive towards all peptidoglycan precursors
-
-
?
additional information
?
-
the enzyme is inactive towards all peptidoglycan precursors
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the purified recombinant enzyme shows no nuclease activity with DNA
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the purified recombinant enzyme shows no nuclease activity with DNA
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
N-acetylmuramic acid is not a substrate. With N-acetylglucosamine as substrate D-glucosamine is formed
-
-
?
additional information
?
-
-
enzyme is inactive against peptidoglycans from Staphylococcus aureus, Staphylococcus carnosus or Escherichia coli. No substrate: N-acetylglucosamine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
additional information
?
-
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
enzymatic deacetylation of chemically acetylated vegetative peptidoglycan from Bacillus cereus by BC1960 and BC3618 results in increased resistance to lysozyme digestion
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
enzymic N-acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in Lactococcus lactis cells, and this leads to decreased cellular autolysis
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
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
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
-
-
-
?
acetylated peptidoglycan + H2O
deacetylated peptidoglycan + acetate
peptidoglycan GlcNAc deacetylase protects the Gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan GlcNAc residues
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
Q81P72, Q81RR3
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
Q81P72, Q81RR3
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
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
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
peptidoglycan N-deacetylation is an important modification of Listeria peptidoglycan, which allows this human pathogen to evade the innate immune system
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
peptidoglycan-N-acetyl-D-glucosamine + H2O
peptidoglycan-D-glucosamine + acetate
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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evolution
peptidoglycan deacetylases (PGNG-dacs) belong to the carbohydrate esterase family 4 (CE4)
evolution
Q81P72, Q81RR3
peptidoglycan deacetylases (PGNG-dacs) belong to the carbohydrate esterase family 4 (CE4)
evolution
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
evolution
-
peptidoglycan deacetylases (PGNG-dacs) belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
peptidoglycan deacetylases (PGNG-dacs) belong to the carbohydrate esterase family 4 (CE4)
-
evolution
-
Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)
-
malfunction
-
evaluation of the DELTApgdA mutant in both the CD1 murine and the porcine models of infection reveals a significant contribution of the pgdA gene to the virulence traits of Streptococcus suis. Reflecting a severe impairment in its ability to persist in blood and decreased ability to escape immune clearance mechanisms mediated by neutrophils, the DELTApgdA mutant is highly attenuated in both models. The results of this study suggest that modification of peptidoglycan by N-deacetylation is an important factor in Streptococcus suis virulence
malfunction
-
inactivation of the wall-associated de-N-acetylase results in greater susceptibility of the cells to induced autolysis
malfunction
-
a pdaC deletion mutant is sensitive to lysozyme treatment
malfunction
Q81P72, Q81RR3
almost 100fold increase in virulence for RDELTAba1977 mutant strain when it is injected in lysM-/- mice
malfunction
-
a pdaC deletion mutant is sensitive to lysozyme treatment
-
malfunction
-
almost 100fold increase in virulence for RDELTAba1977 mutant strain when it is injected in lysM-/- mice
-
physiological function
-
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
physiological function
-
peptidoglycan N-deacetylation is an important modification of Listeria peptidoglycan, which allows this human pathogen to evade the innate immune system
physiological function
-
construction of a mutant pgdA strain and a pgdA-overexpressing strain and comparison of the pharmacokinetics properties of these recombinant strains with that of a wild-type strain, all producing the same model antigen, the human papillomavirus type-16 E7 protein, in the gastrointestinal tract of mice. There is no correlation between survival, at the ileum level, of bacteria intragastrically administered in mice and bacteria sensitivity or resistance to lysozyme. Neither lysozyme-sensitive nor lysozyme-resistant phenotype in Lactococcus lactis enhances significantly the potential of this bacterium as mucosal delivery live vector
physiological function
-
inactivation of SfpgdA enhances Shigella sensitivity to lysozyme. Peptidoglycan purified from the SfpgdA mutant is sensitive to degradation by lysozyme, and the mutant is rapidly killed by polymorphonuclear neutrophils
physiological function
-
mutants lacking N-acetylglucosamine deacetylase Pgd and mutants in both Pgd and O-acetylmuramic acid transferase are attenuated approximately 2 and 3.5 logs, respectively, in vivo. In bone-marrow derived macrophages, the mutants demonstrate intracellular growth defects and increased induction of cytokine transcriptional responses that emanate from a phagosome and the cytosol. Mutants are lysozyme-sensitive and undergo bacteriolysis in the macrophage cytosol, resulting in AIM2-dependent pyroptosis. Each of the in vitro phenotypes is rescued upon infection of LysM macrophages. The addition of extracellular lysozyme to LysM macrophages restores cytokine induction, host cell death, and Listeria monocytogenes growth inhibition. This suggests that extracellular lysozyme can access the macrophage cytosol and act on intracellular lysozyme-sensitive bacteria
physiological function
enzyme BA1961 participates in the biogenesis of the peptidoglycan during both elongation and cell division
physiological function
-
gene pdcA is regulated by an essential two-component system, YycFG, which is associated with cell division
physiological function
the enzyme is required for bacterial evasion to lysozyme and innate immune responses
physiological function
Q81P72, Q81RR3
the enzyme is required for bacterial evasion to lysozyme and innate immune responses, for neutral polysaccharide attachment to peptidoglycan, and for polysaccharide modification
physiological function
Q81P72, Q81RR3
the enzyme is required for bacterial evasion to lysozyme and innate immune responses. Enzyme BA1977 is associated with lateral peptidoglycan synthesis, it is a bona fide peptidoglycan deacetylase involved in resistance to host lysozyme and required for full virulence
physiological function
the enzyme is responsible for a peptidoglycan modification that counteracts the host immune response
physiological function
Helicobacter pylori is equipped with a peptidoglycan deacetylase (PgdA) that confers both pure peptidoglycan and whole bacterial resistance to lysozyme degradation, which hydrolyzes the beta-1,4 bonds in peptidoglycan. Under oxidative stress, PgdA is highly expressed and confers resistance to lysozyme in wild-type cells. Role of aconitase (AcnB) in Helicobacter pylori as a posttranscriptional regulator of the cell wall-modifying enzyme peptidoglycan deacetylase PgdA, apo-AcnB directly interacts with the pgdA transcript to enhance stability and increase deacetylase enzyme expression, which impacts in vivo survival
physiological function
many bacteria modulate and evade the immune defenses of their hosts through peptidoglycan deacetylation. Deacetylation of cell wall peptidoglycan by the recombinant enzyme leads to lysozyme resistance in Mycobacterium smegmatis
physiological function
peptidoglycan deacetylase is the enzyme responsible for a peptidoglycan modification that counteracts the host immune response
physiological function
-
the enzyme is required for bacterial evasion to lysozyme and innate immune responses
-
physiological function
-
enzyme BA1961 participates in the biogenesis of the peptidoglycan during both elongation and cell division
-
physiological function
-
gene pdcA is regulated by an essential two-component system, YycFG, which is associated with cell division
-
physiological function
-
the enzyme is responsible for a peptidoglycan modification that counteracts the host immune response
-
physiological function
-
peptidoglycan deacetylase is the enzyme responsible for a peptidoglycan modification that counteracts the host immune response
-
physiological function
-
Helicobacter pylori is equipped with a peptidoglycan deacetylase (PgdA) that confers both pure peptidoglycan and whole bacterial resistance to lysozyme degradation, which hydrolyzes the beta-1,4 bonds in peptidoglycan. Under oxidative stress, PgdA is highly expressed and confers resistance to lysozyme in wild-type cells. Role of aconitase (AcnB) in Helicobacter pylori as a posttranscriptional regulator of the cell wall-modifying enzyme peptidoglycan deacetylase PgdA, apo-AcnB directly interacts with the pgdA transcript to enhance stability and increase deacetylase enzyme expression, which impacts in vivo survival
-
physiological function
-
many bacteria modulate and evade the immune defenses of their hosts through peptidoglycan deacetylation. Deacetylation of cell wall peptidoglycan by the recombinant enzyme leads to lysozyme resistance in Mycobacterium smegmatis
-
physiological function
-
the enzyme is required for bacterial evasion to lysozyme and innate immune responses, for neutral polysaccharide attachment to peptidoglycan, and for polysaccharide modification
-
physiological function
-
the enzyme is required for bacterial evasion to lysozyme and innate immune responses. Enzyme BA1977 is associated with lateral peptidoglycan synthesis, it is a bona fide peptidoglycan deacetylase involved in resistance to host lysozyme and required for full virulence
-
physiological function
-
construction of a mutant pgdA strain and a pgdA-overexpressing strain and comparison of the pharmacokinetics properties of these recombinant strains with that of a wild-type strain, all producing the same model antigen, the human papillomavirus type-16 E7 protein, in the gastrointestinal tract of mice. There is no correlation between survival, at the ileum level, of bacteria intragastrically administered in mice and bacteria sensitivity or resistance to lysozyme. Neither lysozyme-sensitive nor lysozyme-resistant phenotype in Lactococcus lactis enhances significantly the potential of this bacterium as mucosal delivery live vector
-
additional information
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
additional information
-
catalytic mechanism possibilities analyzed using the mechanism of reaction of acetyl removal from a model substrate, the N-acetylglucosamine/N-acetylmuramic acid dimer by peptidogylcan deacetylase. Analysis via hybrid quantum chemical/molecular mechanical potential calculations (QC/MM), in conjunction with reaction-path-finding algorithms, molecular docking and molecular dynamics simulations, overview. The active site of this enzyme is in a region of highly negative electrostatic potential and contains a zinc dication with a bound water molecule
additional information
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
additional information
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
additional information
-
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
additional information
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
additional information
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
additional information
-
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
-
additional information
-
sequence comparisons of the PGNGdacs BC1960, BA1961, BC1974 and BA1977 from Bacillus cereus and Bacillus anthracis
-
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
-
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
-
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
-
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
-
additional information
-
Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4
-
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Araki, Y.; Fukuoka, S.; Oba, S.; Ito, E.
Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls
Biochem. Biophys. Res. Commun.
45
751-758
1971
Bacillus cereus
brenda
Tsalafouta, A.; Psylinakis, E.; Kapetaniou, E.G.; Kotsifaki, D.; Deli, A.; Roidis, A.; Bouriotis, V.; Kokkinidis, M.
Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6
Acta Crystallogr. Sect. F
64
203-205
2008
Bacillus cereus (Q81EK9), Bacillus cereus
brenda
Araki, Y.; Oba, S.; Araki, S.; Ito, E.
Enzymic deacetylation of N-acetylglucosamine residues in cell wall peptidoglycan
J. Biochem.
88
469-479
1980
Bacillus cereus
brenda
Psylinakis, E.; Boneca, I.G.; Mavromatis, K.; Deli, A.; Hayhurst, E.; Foster, S.J.; Varum, K.M.; Bouriotis, V.
Peptidoglycan N-Acetylglucosamine Deacetylases from Bacillus cereus, Highly Conserved Proteins in Bacillus anthracis
J. Biol. Chem.
280
30856-30863
2005
Bacillus cereus
brenda
Meyrand, M.; Boughammoura, A.; Courtin, P.; Mezange, C.; Guillot, A.; Chapot-Chartier, M.P.
Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis
Microbiology
153
3275-3285
2007
Lactococcus lactis, Lactococcus lactis IL1403
brenda
Blair, D.E.; Schuttelkopf, A.W.; MacRae, J.I.; van Aalten, D.M.F.
Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
Proc. Natl. Acad. Sci. USA
102
15429-15434
2005
Streptococcus pneumoniae (Q8DP63), Streptococcus pneumoniae
brenda
Boneca, I.G.; Dussurget, O.; Cabanes, D.; Nahori, M.A.; Sousa, S.; Lecuit, M.; Psylinakis, E.; Bouriotis, V.; Hugot, J.P.; Giovannini, M.; Coyle, A.; Bertin, J.; Namane, A.; Rousselle, J.C.; Cayet, N.; Prevost, M.C.; Balloy, V.; Chignard, M.; Philpott, D.J.; Cossart, P.; Girardin, S.E.
A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system
Proc. Natl. Acad. Sci. USA
104
997-1002
2007
Listeria monocytogenes
brenda
Wang, G.; Olczak, A.; Forsberg, L.S.; Maier, R.J.
Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori
J. Biol. Chem.
284
6790-6800
2009
Helicobacter pylori
brenda
Popowska, M.; Kusio, M.; Szymanska, P.; Markiewicz, Z.
Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis
J. Microbiol. Biotechnol.
19
932-945
2009
Listeria monocytogenes
brenda
Fittipaldi, N.; Sekizaki, T.; Takamatsu, D.; Dominguez-Punaro Mde, L.; Harel, J.; Bui, N.K.; Vollmer, W.; Gottschalk M.
Significant contribution of the pgdA gene to the virulence of Streptococcus suis
Mol. Microbiol.
70
1120-1135
2008
Streptococcus suis
brenda
Davis, K.M.; Akinbi, H.T.; Standish, A.J.; Weiser, J.N.
Resistance to mucosal lysozyme compensates for the fitness deficit of peptidoglycan modifications by Streptococcus pneumoniae
PLoS Pathog.
4
e1000241
2008
Streptococcus pneumoniae (A0A0H2UQQ3)
brenda
Bui, N.K.; Turk, S.; Buckenmaier, S.; Stevenson-Jones, F.; Zeuch, B.; Gobec, S.; Vollmer, W.
Development of screening assays and discovery of initial inhibitors of pneumococcal peptidoglycan deacetylase PgdA
Biochem. Pharmacol.
82
43-52
2011
Streptococcus pneumoniae
brenda
Rae, C.S.; Geissler, A.; Adamson, P.C.; Portnoy, D.A.
Mutations of the Listeria monocytogenes peptidoglycan N-deacetylase and O-acetylase result in enhanced lysozyme sensitivity, bacteriolysis, and hyperinduction of innate immune pathways
Infect. Immun.
79
3596-3606
2011
Listeria monocytogenes
brenda
Watterlot, L.; Meyrand, M.; Gaide, N.; Kharrat, P.; Blugeon, S.; Gratadoux, J.J.; Flores, M.J.; Langella, P.; Chapot-Chartier, M.P.; Bermudez-Humaran, L.G.
Variations of N-acetylation level of peptidoglycan do not influence persistence of Lactococcus lactis in the gastrointestinal tract
Int. J. Food Microbiol.
144
29-34
2010
Lactococcus lactis
brenda
Kaoukab-Raji, A.; Biskri, L.; Bernardini, M.L.; Allaoui, A.
Characterization of SfPgdA, a Shigella flexneri peptidoglycan deacetylase required for bacterial persistence within polymorphonuclear neutrophils
Microbes Infect.
14
619-627
2012
Shigella flexneri
brenda
Shaik, M.M.; Cendron, L.; Percudani, R.; Zanotti, G.
The structure of Helicobacter pylori HP0310 reveals an atypical peptidoglycan deacetylase
PLoS ONE
6
e19207
2011
Helicobacter pylori (B5ZA76), Helicobacter pylori
brenda
Austin, C.M.; Maier, R.J.
Aconitase-mediated posttranscriptional regulation of Helicobacter pylori peptidoglycan deacetylase
J. Bacteriol.
195
5316-5322
2013
Helicobacter pylori (O25080), Helicobacter pylori, Helicobacter pylori ATCC 700392 (O25080)
brenda
Kobayashi, K.; Sudiarta, I.P.; Kodama, T.; Fukushima, T.; Ara, K.; Ozaki, K.; Sekiguchi, J.
Identification and characterization of a novel polysaccharide deacetylase C (PdaC) from Bacillus subtilis
J. Biol. Chem.
287
9765-9776
2012
Bacillus subtilis, Bacillus subtilis 168
brenda
Balomenou, S.; Fouet, A.; Tzanodaskalaki, M.; Couture-Tosi, E.; Bouriotis, V.; Boneca, I.G.
Distinct functions of polysaccharide deacetylases in cell shape, neutral polysaccharide synthesis and virulence of Bacillus anthracis
Mol. Microbiol.
87
867-883
2013
Bacillus cereus (Q81AF4), Bacillus cereus (Q81EK9), Bacillus anthracis (Q81P72), Bacillus anthracis (Q81RR3), Bacillus anthracis, Bacillus cereus ATCC 14579 (Q81AF4), Bacillus cereus ATCC 14579 (Q81EK9), Bacillus anthracis ATCC 14578 (Q81P72), Bacillus anthracis ATCC 14578 (Q81RR3)
brenda
Munan Shaik, M.; Bhattacharjee, N.; Bhattacharjee, A.; Field, M.; Zanotti, G.
Characterization of the divalent metal binding site of bacterial polysaccharide deacetylase using crystallography and quantum chemical calculations
Proteins
82
1311-1318
2014
Helicobacter pylori (B5ZA76), Helicobacter pylori, Helicobacter pylori G27 (B5ZA76)
brenda
Yang, S.; Zhang, F.; Kang, J.; Zhang, W.; Deng, G.; Xin, Y.; Ma, Y.
Mycobacterium tuberculosis Rv1096 protein: gene cloning, protein expression, and peptidoglycan deacetylase activity
BMC Microbiol.
14
174
2014
Mycobacterium tuberculosis (O53444), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (O53444)
brenda
Giastas, P.; Andreou, A.; Papakyriakou, A.; Koutsioulis, D.; Balomenou, S.; Tzartos, S.J.; Bouriotis, V.; Eliopoulos, E.E.
Structures of the peptidoglycan N-acetylglucosamine deacetylase Bc1974 and its complexes with zinc metalloenzyme inhibitors
Biochemistry
57
753-763
2018
Bacillus cereus (Q81EJ6), Bacillus cereus, Bacillus cereus ATCC 14579 (Q81EJ6), Bacillus cereus NRRL B-3711 (Q81EJ6), Bacillus cereus NCIMB 9373 (Q81EJ6), Bacillus cereus DSM 31 (Q81EJ6), Bacillus cereus NBRC 15305 (Q81EJ6), Bacillus cereus JCM 2152 (Q81EJ6)
brenda
Balomenou, S.; Koutsioulis, D.; Tomatsidou, A.; Tzanodaskalaki, M.; Petratos, K.; Bouriotis, V.
Polysaccharide deacetylases serve as new targets for the design of inhibitors against Bacillus anthracis and Bacillus cereus
Bioorg. Med. Chem.
26
3845-3851
2018
Bacillus anthracis (A0A2B6CE99), Bacillus anthracis (A0A2P0HD08), Bacillus anthracis, Bacillus cereus (Q81EJ6), Bacillus cereus (Q81EK9), Bacillus cereus, Bacillus cereus ATCC 14579 (Q81EJ6), Bacillus cereus ATCC 14579 (Q81EK9)
brenda
Bhattacharjee, N.; Feliks, M.; Shaik, M.M.; Field, M.J.
Catalytic mechanism of peptidoglycan deacetylase a computational study
J. Phys. Chem. B
121
89-99
2017
Helicobacter pylori
brenda