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3-carboxyumbelliferyl acetate + H2O
3-carboxyumbelliferol + acetate
-
-
-
-
?
beta-1,6-linked N-acetylglucosamine hexamer + H2O
partially de-N-acetylated beta-1,6-linked N-acetylglucosamine hexamer + acetate
-
-
-
-
?
beta-1,6-linked N-acetylglucosamine oligomer + H2O
partially de-N-acetylated beta-1,6-linked N-acetylglucosamine oligomer + acetate
-
the enzyme preferentially de-N-acetylates the second residue from the reducing terminus in the pentasaccharide and second and third residues from the reducing terminus in the hexasaccharide
-
-
?
beta-1,6-linked N-acetylglucosamine oligomers + H2O
partially de-N-acetylated beta-1,6-linked N-acetylglucosamine oligomer + acetate
-
specific for the substrate
-
-
?
beta-1,6-linked N-acetylglucosamine pentamer + H2O
partially de-N-acetylated beta-1,6-linked N-acetylglucosamine pentamer + acetate
-
-
-
-
?
beta-1,6-linked N-acetylglucosamine trimer + H2O
partially de-N-acetylated beta-1,6-linked N-acetylglucosamine trimer + acetate
-
-
-
-
?
N-acetylated beta-(1->6)-N-acetylglucosamine polymer + H2O
N-deacetylated beta-(1->6)-N-acetylglucosamine polymer + acetate
-
the enzyme produces partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers
-
-
?
N-acetylated oligogalactosamine + H2O
?
N-acetylated polygalactosamine + H2O
polygalactosamine + acetate
N-acetylgalactosamine + H2O
?
-
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
poly-beta-1,6-N-acetyl-D-glucosamine-adhesin + H2O
acetate + ?
additional information
?
-
N-acetylated oligogalactosamine + H2O
?
-
rate of deacetylation increases with the number of monosaccharide units in the oligosaccharides: with 14 or more N-acetylgalactosamine units: at a rate similar to that of deacetylation of the polymer, trimer to hexamer: slowly, inactive towards disaccharide
-
-
?
N-acetylated oligogalactosamine + H2O
?
-
rate of deacetylation increases with the number of monosaccharide units in the oligosaccharides: with 14 or more N-acetylgalactosamine units: at a rate similar to that of deacetylation of the polymer, trimer to hexamer: slowly, inactive towards disaccharide
-
-
?
N-acetylated polygalactosamine + H2O
polygalactosamine + acetate
-
-
-
-
?
N-acetylated polygalactosamine + H2O
polygalactosamine + acetate
-
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
involved in production of muramic delta-lactam
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
25-kDa protein stimulates CD4+ T cells to develop a protective Th1 response associated with increased IFN-gamma and IL-2 production. The IFN-gamma response, but not the IL-2 response, is apparently required for the protective effects of d25 immunization
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
induces protective immunity responses
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
25-kDa protein stimulates CD4+ T cells to develop a protective Th1 response associated with increased IFN-gamma and IL-2 production. The IFN-gamma response, but not the IL-2 response, is apparently required for the protective effects of d25 immunization
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
enzyme may be involved in determining the properties of the hyphal apex of the colonial form of Neurospora crassa, could play a role in morphogenetic regulation
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
Phage Vi
-
-
-
-
?
poly-beta-1,6-N-acetyl-D-glucosamine-adhesin + H2O
acetate + ?
beta-1,6-GlcNAc (PGA) also called polysaccharide intracellular adhesin (PIA)
-
-
?
poly-beta-1,6-N-acetyl-D-glucosamine-adhesin + H2O
acetate + ?
beta-1,6-GlcNAc (PGA) also called polysaccharide intracellular adhesin (PIA)
-
-
?
additional information
?
-
-
no substrates: bacterial cell wall peptidoglycan, N-acetylated heparin, partially O-hydroxyethylated chitin or monomeric N-acetylgalactosamine derivatives
-
-
?
additional information
?
-
-
no substrates: bacterial cell wall peptidoglycan, N-acetylated heparin, partially O-hydroxyethylated chitin or monomeric N-acetylgalactosamine derivatives
-
-
?
additional information
?
-
-
disruption of enzyme results in formation of spores of dark grey color (phase contrast microscopy) with almost completely lost viability
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation
-
-
?
additional information
?
-
involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation
-
-
?
additional information
?
-
-
development of a fluorogenic assay to monitor the enzyme activity in vitro, overview. Monosaccharides are not substrates of the enzyme
-
-
?
additional information
?
-
involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation
-
-
?
additional information
?
-
involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
-
the enzyme shows metal-dependent N-deacetylase activity on beta-1,6-linked N-acetylglucosamine oligomers with low catalytic efficiency toward the oligomeric substrates. While the enzyme displays similar rates of N-deacetylation with trisaccharide through hexasaccharide beta-1,6-linked N-acetylglucosamine oligomers, position specific de-N-acetylation is only observed with penta- and hexasaccharides
-
-
?
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beta-1,6-linked N-acetylglucosamine oligomers + H2O
partially de-N-acetylated beta-1,6-linked N-acetylglucosamine oligomer + acetate
-
specific for the substrate
-
-
?
N-acetylated beta-(1->6)-N-acetylglucosamine polymer + H2O
N-deacetylated beta-(1->6)-N-acetylglucosamine polymer + acetate
-
the enzyme produces partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
additional information
?
-
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
occurrence of this enzyme may account for the formation of the polygalactosamine with amino groups
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
involved in production of muramic delta-lactam
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
25-kDa protein stimulates CD4+ T cells to develop a protective Th1 response associated with increased IFN-gamma and IL-2 production. The IFN-gamma response, but not the IL-2 response, is apparently required for the protective effects of d25 immunization
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
induces protective immunity responses
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
25-kDa protein stimulates CD4+ T cells to develop a protective Th1 response associated with increased IFN-gamma and IL-2 production. The IFN-gamma response, but not the IL-2 response, is apparently required for the protective effects of d25 immunization
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
-
-
?
N-acetylgalactosaminoglycan + H2O
galactosaminoglycan + acetate
-
enzyme may be involved in determining the properties of the hyphal apex of the colonial form of Neurospora crassa, could play a role in morphogenetic regulation
-
-
?
additional information
?
-
-
disruption of enzyme results in formation of spores of dark grey color (phase contrast microscopy) with almost completely lost viability
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
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Ca2+
-
stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
Co2+
-
pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
Cu2+
-
85% inhibition at 1 mM
dipicolinic acid
-
a metal chelator, complete inhibition
EDTA
-
a metal chelator, complete inhibition
methyl 2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(octanoylsulfanyl)acetyl]amino]-beta-D-lucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
methyl 2-deoxy-2-(sulfamoylamino)-beta-D-glucopyranoside
-
9% inhibition at 1 mM
methyl 2-deoxy-2-[(hydroxyacetyl)(methyl)amino]-beta-D-glucopyranoside
-
84% inhibition at 1 mM
methyl 2-deoxy-2-[(hydroxyacetyl)amino]-beta-D-glucopyranoside
-
8% inhibition at 1 mM
methyl 2-deoxy-2-[(methylsulfonyl)amino]-beta-D-glucopyranoside
-
7% inhibition at 1 mM
methyl 2-deoxy-2-[(sulfanylacetyl)amino]-beta-D-glucopyranoside
-
-
methyl 2-deoxy-2-[methyl(methylsulfonyl)amino]-beta-D-glucopyranoside
-
18% inhibition at 1 mM
methyl 2-deoxy-2-[methyl(sulfamoyl)amino]-beta-D-glucopyranoside
-
67% inhibition at 1 mM
methyl 2-deoxy-2-[methyl(sulfanylacetyl)amino]-beta-D-glucopyranoside
-
48% inhibition at 1 mM
Mg2+
-
pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
Mn2+
-
pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
additional information
-
synthesis and evaluation of a series of enzyme inhibitors, consisting of a metal chelating functional group on a glucosamine scaffold to target the active site metal ion of the enzyme, overview. No or poor inhibitory effect by methyl 2-deoxy-2-(glycylamino)-beta-D-glucopyranoside, methyl 2-deoxy-2-[(hydroxycarbamoyl)amino]-beta-D-glucopyranoside, methyl 2-deoxy-2-[glycyl(methyl)amino]-beta-D-glucopyranoside, and methyl 2-deoxy-2-[(hydroxycarbamoyl)(methyl)amino]-beta-D-glucopyranoside
-
additional information
-
metal chelation to the His-tag of the recombinant enzyme effects N-deacetylation activity
-
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evolution
-
conservation of holdfast synthesis genes in the Caulobacterales clade of the Alphaproteobacteria, gene hfsH is broadly conserved in the hfs gene cluster across several bacterial species
evolution
-
conservation of holdfast synthesis genes in the Caulobacterales clade of the Alphaproteobacteria, gene hfsH is broadly conserved in the hfs gene cluster across several bacterial species
evolution
-
the enzyme belongs to the bacterial family 4 carbohydrate esterases (CE-4) found whose members contain a conserved (alpha/beta)8 fold
evolution
-
the enzyme belongs to the family 4 carbohydrate esterases, CE4
evolution
-
the enzyme belongs to the the carbohydrate esterase family 4, CE4
malfunction
-
disruption of the hfsH gene, which encodes a putative polysaccharide deacetylase, leads to accumulation of polar polysaccharide holdfast in the culture supernatant. The hfsH deletion mutant strain synthesizes holdfast, but the holdfasts are shed into the medium and have decreased adhesiveness and cohesiveness, phenotype, overview. Site-directed mutagenesis at the predicted catalytic site D48 phenocopied the DELTAhfsH mutant and abolishes the esterase activity of the enzyme
malfunction
-
disruption of the hfsH gene, which encodes a putative polysaccharide deacetylase, leads to accumulation of polar polysaccharide holdfast in the culture supernatant. The hfsH deletion mutant strain synthesizes holdfast, but the holdfasts are shed into the medium and have decreased adhesiveness and cohesiveness, phenotype, overview. Site-directed mutagenesis at the predicted catalytic site phenocopied the DELTAhfsH mutant and abolishes the esterase activity of the enzyme
malfunction
-
enzyme deletion causes dramatically reduced biofilm formation in vitro as well as reduced pathogenicity in animal models of biofilm infections
physiological function
A pdi disruption mutant is attenuated for virulence in the hybrid striped bass model and for survival in whole fish blood. Pdi promotes bacterial resistance to lysozyme killing and the ability to adhere to and invade epithelial cells. There is no difference in the autolytic potential, resistance to oxidative killing or resistance to cationic antimicrobial peptides between Streptococcus iniae wild-type and pdi disruption mutant
physiological function
-
in Asticcacaulis biprosthecum, surface attachment and subsequent biofilm growth depend on the ability to synthesize an adhesive polar polysaccharide known as the holdfast, involving the enzyme. The polysaccharide deacetylase activity of HfsH is required for the adhesive and cohesive properties of the holdfast, as well as for the anchoring of the holdfast to the cell envelope, the holdfast contains beta-1,4-N-acetylglucosamine polymers
physiological function
-
in Caulobacter crescentus, surface attachment and subsequent biofilm growth depend on the ability to synthesize an adhesive polar polysaccharide known as the holdfast, involving the enzyme. The polysaccharide deacetylase activity of HfsH is required for the adhesive and cohesive properties of the holdfast, as well as for the anchoring of the holdfast to the cell envelope, the holdfast contains beta-1,4-N-acetylglucosamine polymers
physiological function
-
many medically important biofilm forming bacteria produce similar polysaccharide intercellular adhesins consisting of partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers, in Escherichia coli, de-N-acetylation of the beta-(1->6)-N-acetylglucosamine polymer is catalysed by deacetylase PgaB. N-Deacetylation of the polymers is essential for productive partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymer-dependent biofilm formation
additional information
structure determination and analysis using a molecular replacement procedure, method overview. Contruction of putative models of the C-terminal domain of the protein using a multitude of homology-modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing
additional information
-
structure determination and analysis using a molecular replacement procedure, method overview. Contruction of putative models of the C-terminal domain of the protein using a multitude of homology-modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing
additional information
-
the enzyme has a His-His-Asp metal coordinating triad as well as conserved catalytic residues
additional information
-
the HfsH protein contains 4 conserved motifs, including the essential acetate binding residues and the zinc-binding triad, the enzyme has all the known essential components required to function as polysaccharide deacetylase
additional information
-
the HfsH protein contains 4 conserved motifs, including the essential acetate binding residues and the zinc-binding triad, the enzyme has all the known essential components required to function as polysaccharide deacetylase
additional information
-
the metal-dependent enzyme has a conserved His-His-Asp catalytic triad
additional information
-
structure determination and analysis using a molecular replacement procedure, method overview. Contruction of putative models of the C-terminal domain of the protein using a multitude of homology-modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing
-
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purified enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 24-28 mg/ml protein in 25 mM Tris base, pH 8.0, 300 mM NaCl, and 10% glycerol with 0.002 ml reservoir solution containing 0.1 M Tris base, pH 8.0, 0.2 M NaCl, 30-34% PEG 3350, and equilibration against a 0.5 ml reservoir solution, 1-2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, energy-dispersive X-ray spectroscopy
-
purified recombinant enzyme, hanging drop vapour diffusion, protein in 50 mM HEPES-NaOH, pH 6.8, 200 mM NaCl is mixed with 25-30% w/v PEG 3350, 100 mM Tris-HCl, pH 7.5-8.0, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement procedure, method overview. Construction of putative models of the C-terminal domain of the protein using a multitude of homology modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing
alignment with PDB database: hits to tetratricopeptide repeat domains of human nucleoporin O-linked N-acetylglucosamine transferase, yeast mitochondrial outer membrane translocon protein Tom70p, and human peroxisomal targeting signal-1 receptor PEX5, putative domains: porin domain for export of poly-beta-1,6-N-acetyl-D-glucosamine, and periplasmic domain for protein-protein interactions
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D48A
-
site-directed mutagenesis of the catalytic residue abolishes the esterase activity of the enzyme, the mutant strain is deficient in holdfast anchoring to the cell body, and small holdfasts are shed into the medium. The mutant enzyme has a similar secondary structure compared to the wild-type enzyme based on circular dichroism measurement
D115A
decreased catalytic activity, 6.4% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin
H184A
mutant, deficient in biofilm formation
PgaB271
DUF187 domain truncation mutant, amino acids 1-271, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 4.1% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin
PgaB410
DUF187 domain truncation mutant, amino acids 1-410, proteolytic cleavage during overexpression
PgaB516
DUF187 domain truncation mutant, amino acids 1-516, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 5% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin, proteolytic cleavage during overexpression
D115A
-
decreased catalytic activity, 6.4% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin
-
H184A
-
mutant, deficient in biofilm formation
-
PgaB271
-
DUF187 domain truncation mutant, amino acids 1-271, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 4.1% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin
-
PgaB410
-
DUF187 domain truncation mutant, amino acids 1-410, proteolytic cleavage during overexpression
-
PgaB516
-
DUF187 domain truncation mutant, amino acids 1-516, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 5% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin, proteolytic cleavage during overexpression
-
additional information
-
deletion of gene hfsH abolishing surface adhesion of the cell. The gene hfsH deletion mutant synthesizes defective holdfasts with low adhesiveness and cohesiveness that cannot be anchored to the cell body. In contrast, overexpression of HfsH increases cell adherence. Phenotypes of Asticcacaulis biprosthecum transposon mutants with insertions in a number of hfs genes, overview
additional information
-
deletion of gene hfsH abolishing surface adhesion of the cell. The gene hfsH deletion mutant synthesizes defective holdfasts with low adhesiveness and cohesiveness that cannot be anchored to the cell body. In contrast, overexpression of HfsH increases cell adherence
additional information
-
enzyme deletion by transposon mutagenesis of gene icaB
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Jorge, J.A.; Kinney, S.G.; Reissig, J.L.
Purification and characterization of Neurospora crassa N-acetyl galactosaminoglycan deacetylase
Braz. J. Med. Biol. Res.
15
29-34
1982
Neurospora crassa
brenda
Araki, Y.; Takada, H.; Fujii, N.; Ito, E.
A pathway of polygalactosamine formation in Aspergillus parasiticus: enzymatic deacetylation of N-acetylated polygalactosamine
Eur. J. Biochem.
102
35-42
1979
Aspergillus oryzae, Aspergillus parasiticus, Aspergillus oryzae AHU 7139, Aspergillus parasiticus AHU 7165
brenda
Kwiatkowski, B.; Jastrzemske, K.B.
Acetylated peptic acid is a sustrate of Vi phages deacetylase
Biochem. Biophys. Res. Commun.
91
730-738
1979
Phage Vi
brenda
Biondo, C.; Beninati, C.; Bombaci, M.; Messina, L.; Mancuso, G.; Midiri, A.; Galbo, R.; Teti, G.
Induction of T helper type 1 responses by a polysaccharide deacetylase from Cryptococcus neoformans
Infect. Immun.
71
5412-5417
2003
Cryptococcus neoformans, Cryptococcus neoformans Filobasidiella neoformans
brenda
Biondo, C.; Beninati, C.; Delfino, D.; Oggioni, M.; Mancuso, G.; Midiri, A.; Bombaci, M.; Tomaselli, G.; Teti, G.
Identification and cloning of a Cryptococcal deacetylase that produces protective immune responses
Infect. Immun.
70
2383-2391
2002
Cryptococcus neoformans (Q96TR5), Cryptococcus neoformans
brenda
Fukushima, T.; Yamamoto, H.; Atrih, A.; Foster, S.J.; Sekiguchi, J.
A polysaccharide deacetylase gene (pdaA) is required for germination and for production of muramic delta-lactam residues in the spore cortex of Bacillus subtilis
J. Bacteriol.
184
6007-6015
2002
Bacillus subtilis
brenda
Jorge, J.A.; De Almeida, E.M.; De Lourdes Polizeli, M.; Terenzi, H.F.
Changes in N-acetylgalactosaminoglycan deacetylase levels during growth of Neurospora crassa: effect of L-sorbose on enzyme production
J. Basic Microbiol.
39
337-344
1999
Neurospora crassa
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Fukushima, T.; Tanabe, T.; Yamamoto, H.; Hosoya, S.; Sato, T.; Yoshikawa, H.; Sekiguchi, J.
Characterization of a polysaccharide deacetylase gene homologue (pdaB) on sporulation of Bacillus subtilis
J. Biochem.
136
283-291
2004
Bacillus subtilis
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Itoh, Y.; Rice, J.D.; Goller, C.; Pannuri, A.; Taylor, J.; Meisner, J.; Beveridge, T.J.; Preston, J.F.; Romeo, T.
Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine
J. Bacteriol.
190
3670-3680
2008
Escherichia coli (P69434), Escherichia coli (P75906), Escherichia coli K-12 MG1655 (P69434), Escherichia coli K-12 MG1655 (P75906)
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Milani, C.J.; Aziz, R.K.; Locke, J.B.; Dahesh, S.; Nizet, V.; Buchanan, J.T.
The novel polysaccharide deacetylase homologue Pdi contributes to virulence of the aquatic pathogen Streptococcus iniae
Microbiology
156
543-554
2010
Streptococcus iniae (C8YNM0), Streptococcus iniae
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Fadouloglou, V.E.; Kapanidou, M.; Agiomirgianaki, A.; Arnaouteli, S.; Bouriotis, V.; Glykos, N.M.; Kokkinidis, M.
Structure determination through homology modelling and torsion-angle simulated annealing: application to a polysaccharide deacetylase from Bacillus cereus
Acta Crystallogr. Sect. D
69
276-283
2013
Bacillus cereus (Q81IM3), Bacillus cereus, Bacillus cereus ATCC 14579 (Q81IM3)
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Strunk, R.; Piemonte, K.; Petersen, N.; Koutsioulis, D.; Bouriotis, V.; Perry, K.; Cole, K.
Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis
Acta Crystallogr. Sect. F
70
156-159
2014
Bacillus anthracis
brenda
Pokrovskaya, V.; Poloczek, J.; Little, D.; Griffiths, H.; Howell, P.; Nitz, M.
Functional characterization of Staphylococcus epidermidis IcaB, a de-N-acetylase important for biofilm formation
Biochemistry
52
5463-5471
2013
Staphylococcus epidermidis
brenda
Wan, Z.; Brown, P.J.; Elliott, E.N.; Brun, Y.V.
The adhesive and cohesive properties of a bacterial polysaccharide adhesin are modulated by a deacetylase
Mol. Microbiol.
88
486-500
2013
Caulobacter vibrioides, Asticcacaulis biprosthecium
brenda
Chibba, A.; Poloczek, J.; Little, D.J.; Howell, P.L.; Nitz, M.
Synthesis and evaluation of inhibitors of E. coli PgaB, a polysaccharide de-N-acetylase involved in biofilm formation
Org. Biomol. Chem.
10
7103-7107
2012
Escherichia coli
brenda