Reference on EC 3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Campbell, P.; Laurent, T.C.; Roden, L.
Assay and properties of N-acetylglucosamine-6-phosphate deacetylase from rat liver
Anal. Biochem.
166
134-141
1987
Rattus norvegicus
Corner, B.E.; Poulter, R.T.M.; Shepherd, M.G.; Sullivan, P.A.
A Candida albicans mutant impaired in the utilization of N-acetylglucosamine
J. Gen. Microbiol.
132
15-19
1986
Candida albicans
Gopal, P.; Sullivan, P.A.; Shepherd, M.G.
Enzymes of N-acetylglucosamine metabolism during germ-tube formation in Candida albicans
J. Gen. Microbiol.
128
2319-2326
1982
Candida albicans
White, R.J.; Pasternak, C.A.
The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli
Biochem. J.
105
121-125
1967
Escherichia coli
Gopal, P.K.; Sullivan, P.A.; Shepherd, M.G.
A rapid and sensitive assay for N-acetylglucosamine-6-phosphate deacetylase
Anal. Biochem.
115
30-33
1981
Candida albicans
White, R.J.; Pasternak, C.A.
N-Acetylglucosamine-6-phosphate deacetylase and glucosamine-6-phosphate deaminase from Escherichia coli
Methods Enzymol.
41
497-502
1975
Bacillus subtilis, Bifidobacterium bifidum, Bos taurus, Escherichia coli
Yamano, N.; Matsushita, Y.; Kamada, K.; Fujishima, S.; Arita, M.
Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholera Non-O1
Biosci. Biotechnol. Biochem.
60
1320-1323
1996
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 Non-O1
Ferreira, F.M.; Mendoza-Hernandez, M.L.; Calcagno, F.; Minauro, L.F.; Delboni, L.F.; Oliva, G.
Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli
Acta Crystallogr. Sect. D
56
670-672
2000
Escherichia coli
-
Souza, J.M.; Plumbridge, J.A.; Calcagno, M.L.
N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization
Arch. Biochem. Biophys.
340
338-346
1997
Escherichia coli, Escherichia coli overproducing
Weidanz, J.A.; Campbell, P.; Moore, D.; deLucas, L.J.; Roden, L.; Thompson, J.N.; Vezza, P.
N-Acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium falciparum
Br. J. Haematol.
95
645-653
1996
Homo sapiens, Plasmodium falciparum
Campbell, P.; Thompson, J.N.; Fraser, J.R.; Laurent, T.C.; Pertoft, H.; Roden, L.
N-Acetylglucosamine-6-phosphate deacetylase in hepatocytes, Kupffer cells and sinusoidal endothelial cells from rat liver
Hepatology
11
199-204
1990
Homo sapiens, Rattus norvegicus
Yamano, N.; Higashida, N.; Endo, C.; Sakata, N.; Fujishima, S.; Maruyama, A.; Higashihara, T.
Purification and characterization of N-acetylglucosamine-6-phosphate deacetylase from a psychrotrophic marine bacterium, Alteromonas species
Mar. Biotechnol.
2
57-64
2000
Alteromonas sp., Vibrio cholerae serotype O1
Vincent, F.; Yates, D.; Garman, E.; Davies, G.J.; Brannigan, J.A.
The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily
J. Biol. Chem.
279
2809-2816
2004
Bacillus subtilis
Xu, C.; Hall, R.; Cummings, J.; Raushel, F.M.
Tight binding inhibitors of N-acyl amino sugar and N-acyl amino acid deacetylases
J. Am. Chem. Soc.
128
4244-4245
2006
Escherichia coli
Alvarez-Anorve, L.I.; Calcagno, M.L.; Plumbridge, J.
Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates
J. Bacteriol.
187
2974-2982
2005
Escherichia coli
Ferreira, F.M.; Mendoza-Hernandez, G.; Castaneda-Bueno, M.; Aparicio, R.; Fischer, H.; Calcagno, M.L.; Oliva, G.
Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli
J. Mol. Biol.
359
308-321
2006
Escherichia coli (P0AF18), Escherichia coli
Hall, R.S.; Xiang, D.F.; Xu, C.; Raushel, F.M.
N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion
Biochemistry
46
7942-7952
2007
Escherichia coli (P0AF18), Escherichia coli
Hall, R.S.; Brown, S.; Fedorov, A.A.; Fedorov, E.V.; Xu, C.; Babbitt, P.C.; Almo, S.C.; Raushel, F.M.
Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase
Biochemistry
46
7953-7962
2007
Thermotoga maritima, Escherichia coli (P0AF18), Escherichia coli
May, M.; Brown, D.R.
Genetic variation in sialidase and linkage to N-acetylneuraminate catabolism in Mycoplasma synoviae
Microb. Pathog.
45
38-44
2008
Mycoplasmopsis synoviae
Wendland, J.; Schaub, Y.; Walther, A.
N-Acetylglucosamine utilization by Saccharomyces cerevisiae based on expression of Candida albicans NAG genes
Appl. Environ. Microbiol.
75
5840-5845
2009
Candida albicans
Plumbridge, J.
An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in Escherichia coli
J. Bacteriol.
191
5641-5647
2009
Escherichia coli
Popowska, M.; Osinska, M.; Rzeczkowska, M.
N-acetylglucosamine-6-phosphate deacetylase (NagA) of Listeria monocytogenes EGD, an essential enzyme for the metabolism and recycling of amino sugars
Arch. Microbiol.
194
255-268
2012
Listeria monocytogenes (Q8Y5F6), Listeria monocytogenes (Q8Y8E8), Listeria monocytogenes
Yadav, V.; Panilaitis, B.; Shi, H.; Numuta, K.; Lee, K.; Kaplan, D.L.
N-acetylglucosamine 6-phosphate deacetylase (nagA) is required for N-acetyl glucosamine assimilation in Gluconacetobacter xylinus
PLoS ONE
6
e18099
2011
Komagataeibacter xylinus (D2KKE6), Komagataeibacter xylinus, Komagataeibacter xylinus 10245 (D2KKE6)
Choi, C.W.; An, H.Y.; Lee, Y.J.; Lee, Y.G.; Yun, S.H.; Park, E.C.; Hong, Y.; Kim, G.H.; Park, J.E.; Baek, S.J.; Kim, H.S.; Kim, S.I.
Characterization of Streptococcus pneumoniae N-acetylglucosamine-6-phosphate deacetylase as a novel diagnostic marker
J. Microbiol.
51
659-664
2013
Streptococcus pneumoniae (Q8DN83), Streptococcus pneumoniae, Streptococcus pneumoniae BAA-255 (Q8DN83)
Davies, J.S.; Coombes, D.; Horne, C.R.; Pearce, F.G.; Friemann, R.; North, R.A.; Dobson, R.C.J.
Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus
FEBS Lett.
593
52-66
2019
Staphylococcus aureus, Staphylococcus aureus USA300_TCH1516
Ahangar, M.S.; Furze, C.M.; Guy, C.S.; Cooper, C.; Maskew, K.S.; Graham, B.; Cameron, A.D.; Fullam, E.
Structural and functional determination of homologs of the Mycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA)
J. Biol. Chem.
293
9770-9783
2018
Mycobacterium marinum (A0A3E2N0G4), Mycobacterium marinum, Mycolicibacterium smegmatis (A0A8B4QF55), Mycolicibacterium smegmatis
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