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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ph-dac, glucosaminyl n-deacetylase, n-acetylglucosamine deacetylase, tk-dac, dacph, ph0499, lmo0415,
more
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acetylaminodeoxyglucose acetylhydrolase
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glucosaminyl N-deacetylase
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N-acetyl-D-glucosaminyl N-deacetylase
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Dacph
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pgdA
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Ph-Dac
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PH0499
locus name
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N-acetyl-D-glucosamine + H2O = D-glucosamine + acetate
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hydrolysis of amide bond
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N-acetyl-D-glucosamine amidohydrolase
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N-acetyl-D-galactosamine + H2O
galactosamine + acetate
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
N-acetyl-D-galactosamine + H2O
galactosamine + acetate
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?
N-acetyl-D-galactosamine + H2O
galactosamine + acetate
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?
N-acetyl-D-galactosamine + H2O
galactosamine + acetate
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?
N-acetyl-D-galactosamine + H2O
galactosamine + acetate
Vibrio cholerae serotype O1 non-O1 1148A
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is involved in chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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the enzyme is involved in chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is involved in chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is involved in chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is probably involved in archaeal chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
Vibrio cholerae serotype O1 non-O1 1148A
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is involved in chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
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the enzyme is involved in chitin catabolic pathway
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N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is involved in chitin catabolic pathway
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?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
the enzyme is probably involved in archaeal chitin catabolic pathway
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?
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Diabetes Mellitus
Diabetes mellitus induced inhibition of glucosaminyl N-deacetylase: effect of short-term blood glucose control in diabetic rats.
Diabetic Angiopathies
Diabetes mellitus induced inhibition of glucosaminyl N-deacetylase: effect of short-term blood glucose control in diabetic rats.
Diabetic Nephropathies
Glucosaminyl N-deacetylase in cultured fibroblasts; comparison of patients with and without diabetic nephropathy, and identification of a possible mechanism for diabetes-induced N-deacetylase inhibition.
Diabetic Nephropathies
Inhibition of glomerular glucosaminyl N-deacetylase in diabetic rats.
Mastocytoma
cDNA cloning and sequencing of mouse mastocytoma glucosaminyl N-deacetylase/N-sulfotransferase, an enzyme involved in the biosynthesis of heparin.
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120 - 127
N-acetyl-D-glucosamine
120
N-acetyl-D-glucosamine
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127
N-acetyl-D-glucosamine
pH 8.5, 75°C
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0.53
N-acetyl-D-glucosamine
pH 8.5, 75°C
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6 - 9.5
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pH 6: 5% of maximal activity, pH 9.5: 10% of maximal activity
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brenda
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brenda
B
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brenda
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
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UniProt
brenda
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brenda
R36A
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brenda
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SwissProt
brenda
non-O1 1148A
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brenda
Vibrio cholerae serotype O1 non-O1 1148A
non-O1 1148A
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brenda
ATCC 4157
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brenda
B
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brenda
stain K-12
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brenda
female Sprague-Dawley rat of the U and H substrain
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brenda
male Sprague-Dawley rat
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brenda
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brenda
R36A
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brenda
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brenda
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brenda
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brenda
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malfunction
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the pgdA-knockout strain shows a significant increase in aggregation/agglutination by salivary agglutinin
malfunction
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in bone-marrow derived macrophages, N-acetylglucosamine deacetylase and O-acetylmuramic acid transferase double-deficient mutants demonstrate intracellular growth defects and increased induction of cytokine transcriptional responses that emanated from a phagosome and the cytosol. N-acetylglucosamine deacetylase deficient Listeria monocytogenes bacteria are sensitive to 0.05 mg/ml lysozyme, undergo increased bacteriolysis in the macrophage cytosol, induce AIM2-dependent pyroptosis and increased vacuolar and cytosolic cytokine signaling, demonstrate intracellular growth defects that are rescued in the absence of lysozyme M and in vivo defects that are not rescued in the absence of lysozyme M
malfunction
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inactivation of the N-acetylglucosamine deacetylase gene leads to fully acetylated peptidoglycan, resulting in a lysozyme-sensitive phenotype
malfunction
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inactivation of the N-acetylglucosamine deacetylase gene leads to fully acetylated peptidoglycan, resulting in a lysozyme-sensitive phenotype
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physiological function
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PgdA is an active, metal-dependent CE4 esterase that plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin
physiological function
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N-acetylglucosamine deacetylase gene overexpression leads to an increased degree of peptidoglycan deacetylation, resulting in a lysozyme-resistant phenotype. N-Acetylglucosamine deacetylase does not confer any advantage in the persistence of Lactococcus lactis in the gastrointestinal tract and its ability to enhance host immune responses induced by delivered antigen in situ
physiological function
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N-acetylglucosamine deacetylase gene overexpression leads to an increased degree of peptidoglycan deacetylation, resulting in a lysozyme-resistant phenotype. N-Acetylglucosamine deacetylase does not confer any advantage in the persistence of Lactococcus lactis in the gastrointestinal tract and its ability to enhance host immune responses induced by delivered antigen in situ
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A2RAW2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
309
2
35071
TrEMBL
Secretory Pathway (Reliability: 3 )
A2QVC6_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
459
0
49857
TrEMBL
Mitochondrion (Reliability: 5 )
A1K7Y6_AZOSB
Azoarcus sp. (strain BH72)
279
0
30958
TrEMBL
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O58235_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
272
0
31595
TrEMBL
Mitochondrion (Reliability: 5 )
DCHI_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
267
0
30302
Swiss-Prot
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PGDA_STRR6
463
1
52675
Swiss-Prot
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A1JJJ9_YERE8
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
311
0
34860
TrEMBL
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30000
6 * 30000, SDS-PAGE
31595
6 * 31595, calculated from sequence
31600
x * 31600, SDS-PAGE
52700
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calculation from sequence of DNA
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?
x * 31600, SDS-PAGE
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x * 31600, SDS-PAGE
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homohexamer
6 * 31595, calculated from sequence
homohexamer
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6 * 31595, calculated from sequence
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homohexamer
6 * 30000, SDS-PAGE
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additional information
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nonfunctional enzyme mutant, hypersensitive to exogenous lysozymem reduced virulence
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1°C, 4 h, complete loss of activity
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expression analysis through RT-PCR
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expression in Escherichia coli
expression of a combined glucosaminyl N-deacetylase/N-sulfotransferase in human kidney cell line 293
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overexpressed as inclusion bodies in Escherichia coli Rosetta (DE3) pLys. The insoluble inclusion body is solubilized and reactivated through a refolding procedure
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the transcription is specifically induced by N,N'-diacetylchitobiose, suggesting the function of this gene in chitin catabolism in vivo. N-acetyl-D-glucosamine can not act as an inducer
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medicine
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nonfunctional enzyme mutant, reduced virulence in intraperitoneal mouse model
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Roseman, S.
Glucosamine metabolism. N-acetylglucosamine deacetylase
J. Biol. Chem.
226
115-124
1957
Clostridium cadaveris, Enterococcus faecalis, Escherichia coli, Escherichia coli B / ATCC 11303, Saccharomyces cerevisiae
brenda
Unger, E.; Pettersson, I.; Eriksson, U.J.; Lindahl, U.; Kjellen, L.
Decreased activity of the heparan sulfate-modifying enzyme glucosaminyl N-deacetylase in hepatocytes from streptozotocin-diabetic rats
J. Biol. Chem.
266
8671-8674
1991
Rattus norvegicus
brenda
Yamano, N.; Fujishima, S.; Miwatani, R.; Yuku, F.; Tanaka, R.; Arita, M.
Production of N-acetylglucosamine deacetylase by Vibrio cholerae non-O1
Biosci. Biotechnol. Biochem.
58
193-195
1994
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 non-O1 1148A
brenda
Cheung, W.F.; Eriksson, I.; Kusche-Gulberg, M.; Lindahl, U.; Kjellen, L.
Expression of mouse mastocytoma glucosaminyl N-deacetylase/N-sulfotransferase in human kidney 293 cells results in increased N-sulfation of heparan sulfate
Biochemistry
35
5250-5256
1996
Mus musculus
brenda
Oturai, P.; Deckert, M.; Rolin, B.; Jensen, T.; Kofoed-Enevoldsen, A.
Glucosaminyl N-deacetylase mRNA expression in diabetic rats
Exp. Clin. Endocrinol. Diabetes
107
453-456
1999
Rattus norvegicus
brenda
Vollmer, W.; Tomasz, A.
The pgdA gene encodes for a peptidoglucan N-acetylglucosamine deacetylase in Streptococcus pneumoniae
J. Biol. Chem.
27
20496-20501
2000
Streptococcus pneumoniae, Streptococcus pneumoniae R36A
brenda
Vollmer, W.; Tomasz, A.
Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae
Infect. Immun.
70
7176-7178
2002
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, Lactococcus lactis JIM7049
brenda
Tanaka, T.; Fukui, T.; Fujiwara, S.; Atomi, H.; Imanaka, T.
Concerted action of diacetylchitobiose deacetylase and exo-beta-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
J. Biol. Chem.
279
30021-30027
2004
Thermococcus kodakarensis (Q6F4N1)
brenda
Mine, S.; Ikegami, T.; Kawasaki, K.; Nakamura, T.; Uegaki, K.
Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii
Protein Expr. Purif.
84
265-269
2012
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58235)
brenda
Liu, B.; Ni, J.F.; Shen, Y.L.
Cloning, expression and biochemical characterization of a novel diacetylchitobiose deacetylase from the hyperthermophilic archaeon Pyrococcus horikoshii
Wei Sheng Wu Xue Bao
46
255-258
2006
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58235)
brenda
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