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Information on EC 3.5.1.104 - peptidoglycan-N-acetylglucosamine deacetylase
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3.5.1.104 peptidoglycan-N-acetylglucosamine deacetylaseIUBMB Comments
Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively .
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Word Map
- 3.5.1.104
- lysozyme
-
deacetylation
- streptococcus
- pylori
- helicobacter
- chitin
- cereus
- listeria
- monocytogenes
- anthracis
- muropeptides
-
lysozyme-induced
- chitooligosaccharides
- autolysins
-
de-n-acetylation
-
n-acetylmuramic
- pharmacology
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
peptidoglycan deacetylase, hp310, sfpgda, peptidoglycan n-acetylglucosamine deacetylase, sppgda, bc1960, glcnac deacetylase, bc1974, ba1977, ba1961, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BA1977
BA2944
BC1960
Bc1974
BC3618
GlcNAc deacetylase
HP0310
HpPgdA
MurNAc deacetylase
PdaC
peptidoglycan deacetylase
peptidoglycan GlcNAc deacetylases
peptidoglycan N-acetylglucosamine deacetylase
pgdA
PGNG-dac
PGNGdacs
polysaccharide deacetylase
polysaccharide deacetylase C
Rv1096 protein
YjeA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
peptidoglycan-N-acetylglucosamine amidohydrolase
Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3].
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CAS REGISTRY NUMBER
COMMENTARY
75217-01-5
-
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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
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + 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
-
-
?
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
-
-
-
?
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 from Streptococcus suis + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
peptidoglycan from wild-type Streptococcus pneumoniae + H2O
deacetylated peptidoglycan + acetate
-
-
-
-
?
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
?
-
-
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
-
-
?
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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
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
abolishes the acnB-pgdA transcript binding leading to destabilization of the enzyme's mRNA
Zn2+
additional information
Zn2+
-
lower dependence on zinc or nickel ions for deacetylation of peptidoglycan by the enzyme than other metal ions, Mn2+, Mg2+, and Ca2+
Zn2+
the zinc ion of the metalloenzyme is coordinated by a conserved binding triad of amino acids consisting of one aspartate and two histidine residues, determination of the metal-binding site, which is essential for the enzyme's catalytic activity, one metal site per monomer, structure and quantum chemical calculations of models, overview. The metal ion occupies a tetrahedral environment with binding to one of the carboxylic oxygen of Asp14, His86, His90 and a water molecule
Zn2+
divalent metal binding site, one site per enzyme monomer, essential for the enzyme's catalytic activity, structure analysis, detailed overview
additional information
metal site models show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur, e.g. Fe2+, Co2+, Cu2+, Mg2+, quantum chemical calculations, overview
additional information
-
metal site models show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur, e.g. Fe2+, Co2+, Cu2+, Mg2+, quantum chemical calculations, overview
additional information
SpPgdA is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively
additional information
-
SpPgdA is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[[4-(diethylamino)-2-hydroxyphenyl]carbonyl]benzoic acid
-
1 mM, 7% residual activity
N-(3-acetylphenyl)-2-[2-(hydrazinylcarbonothioyl)hydrazinyl]-2-(1-oxido-3-oxo-3,4-dihydro-2H-1,4-benzothiazin-2-yl)acetamide
-
1 mM, 29% residual activity
additional information
-
the enzyme mutant is sensitive to lysozyme, the growth rate is decreased
-
N-hydroxy-4-(naphthalene-1-yl)benzamide
a potent competitive inhibitor; a potent competitive inhibitor
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Modification of Helicobacter pylori peptidoglycan enhances NOD1 activation and promotes cancer of the stomach.
Pneumonia
Monosaccharide inhibitors targeting carbohydrate esterase family 4 de-N-acetylases.
Tuberculosis
Mycobacterium tuberculosis Rv1096 protein: gene cloning, protein expression, and peptidoglycan deacetylase activity.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3 - 0.45
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
6.2
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
mutant enzyme K304I
26
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
mutant enzyme I419G
0.37
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
enzyme BC1960
0.5
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
-
0.3
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
enzyme BC1960
0.45
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
-
0.91
peptidoglycan-N-acetyl-D-glucosamine
recombinant enzyme, pH 7.0, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
mutant enzyme I419G
1.5
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
mutant enzyme L302A
1.6
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
mutant enzyme K304I
0.099
peptidoglycan-N-acetyl-D-glucosamine
recombinant enzyme, pH 7.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.088
peptidoglycan-N-acetyl-D-glucosamine
recombinant enzyme, pH 7.0, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetic analysis
-
additional information
additional information
inhibition kinetic analysis
-
additional information
additional information
-
inhibition kinetic analysis
-
additional information
additional information
inhibition kinetic analysis
-
additional information
additional information
inhibition kinetic analysis
-
additional information
additional information
-
inhibition kinetic analysis
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2-[[4-(diethylamino)-2-hydroxyphenyl]carbonyl]benzoic acid
Streptococcus pneumoniae
-
37°C, pH 7.0
0.584
N-(3-acetylphenyl)-2-[2-(hydrazinylcarbonothioyl)hydrazinyl]-2-(1-oxido-3-oxo-3,4-dihydro-2H-1,4-benzothiazin-2-yl)acetamide
Streptococcus pneumoniae
-
37°C, pH 7.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
competition experiments with wild-type and mutant strains in lysozyme M-sufficient mice, effect of peptidoglycan modifying enzymes on growth, viability and hydrolysis of pneumococcal cell walls as well as on relative fitness during murine colonization in the presence or absence of lysozyme shown, contribution of lysozyme from neutrophils to survival and colonization of mutants lacking peptidoglycan modifications, effect of peptidoglycan modifying enzymes on expression of capsular polysaccharide (CPS)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and pgdA mutant strains (pgdA and pgdAadr)
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
peptidoglycan modifications during colonizing the mucosal surface of the upper respiratory tract, lysozyme M-sufficient mice
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme does not possess a signal peptide
-
brenda
additional information
the enzyme does not possess a signal peptide
-
brenda
additional information
-
the enzyme does not possess a signal peptide
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
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
Q81P72, Q81RR3
almost 100fold increase in virulence for RDELTAba1977 mutant strain when it is injected in lysM-/- mice
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
-
Show AA Sequence and Transmembrane Helices (818 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
additional information
additional information
-
enzyme domain structure and structure comparisons, overview
additional information
-
enzyme domain structure and structure comparisons, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of Zn-bound and acetate-bound Bc1974 enzyme, PDB ID 5N1J, structure comparisons. Analysis of X-ray crystal structures of the NodB domain of Bc1974, the conserved catalytic core of CE4s, in the unliganded form and in complex with four known metalloenzyme inhibitors and two amino acid hydroxamates that target the active site metal
hanging-drop vapour diffusion method, enzyme is crystallized in the presence of (GlcNAc)6
purified recombinant N-terminally His6-tagged enzyme, vapor diffusion technique, mixing of 18 mg/ml protein solution with 0.2 M ammonium sulfate, 0.1 M tris sodium citrate, pH 5.6, and 15% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified recombinant N-terminally His6-tagged enzyme, vapor diffusion technique, mixing of 18 mg/ml protein solution with precipitant solution containing 0.2 M ammonium sulfate, 0.1 M tris sodium citrate, pH 5.6, and 15% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement and modeling
to 2.57 A resolution. The polypeptide folds into a single domain, characterized by a non-canonical TIM-barrel fold. Nine beta-strands are arranged in a central barrel surrounded by six alpha-helices. Four monomers are present in the asymmetric unit, arranged around a four-fold rotation axis
sitting-drop vapor diffusion method, native crystal structure and product complexes of SpPgdA
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L222V
-
mutant exhibits sensitivity to lysozyme similar to wild-type, acticity is similar to wild-type
additional information
additional information
Q81P72
constructure of a knockout DELTABA2944 mutant
additional information
Q81RR3
constructure of a knockout DELTABA2944 mutant
additional information
construction of Bacillus anthracis 7702 DELTAba1977 mutant strain
additional information
construction of Bacillus anthracis 7702 DELTAba1977 mutant strain
additional information
-
construction of Bacillus anthracis 7702 DELTAba1977 mutant strain
additional information
-
constructure of a knockout DELTABA2944 mutant
-
additional information
-
construction of a conditional null mutant of pdaC: the concatenated pM4SD-PdaC is derived from Escherichia coli strain C600 and Bacillus subtilis strain 168 is transformed with the plasmid by single crossing over recombination, resulting in the PdaCp strain
additional information
-
construction of a conditional null mutant of pdaC: the concatenated pM4SD-PdaC is derived from Escherichia coli strain C600 and Bacillus subtilis strain 168 is transformed with the plasmid by single crossing over recombination, resulting in the PdaCp strain
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged truncated enzyme from Escherichia coli strain JM109 by affinity chromatography and dialysis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of pgdA on a multicopy plasmid vector results in an increased degree of peptidoglycan deacetylation
-
expression in Escherichia coli
gene hp0310, sequence comparison, recombinant expression of N-terminally His6-tagged enzyme
gene pdcA, overexpression of His-tagged truncated enzyme, lacking the transmembrane region, in Escherichia coli strain JM109, subcloning in Escherichia coli strain C600
-
gene pgdA, in the wild type, pgdAmRNAhalf-life is 13 min, whereas the half-life for the acnB strain is 7 min, apo-AcnB binds to the 3'-untranslated region of the pgdA RNA transcript. AcnB-pgdA transcript binding is abolished by the addition of iron. Real-time quantitative PCR enzyme expression analysis and RNA footprinting
gene Rv1096, sequence comparisons, recombinant expression in Escherichia coli strain ER2566 and in Mycobacterium smegmatis strain mc2155, deacetylation of cell wall peptidoglycan by the recombinant enzyme leads to lysozyme resistance in Mycobacterium smegmatis
generation of mutant (pgdA and pgdAadr) and revertant strains
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the pgdA gene is increased upon interaction of the bacterium with neutrophils in vitro as well as in vivo in experimentally inoculated mice
-
PgdA is highly expressed under oxidative stress
SfPgdA expression is controlled by PhoP, a phoP mutant does not produce SfPgdA, which results in increased sensitivity to lysozyyme
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
studies on peptidoglycan modifications by Streptococcus pneumoniae
medicine
-
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
medicine
-
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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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