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Information on EC 3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase and Organism(s) Escherichia coli and UniProt Accession P0AF18
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EC Tree
3.5.1.25 N-acetylglucosamine-6-phosphate deacetylaseSpecify your search results
Word Map
- 3.5.1.25
- deaminase
- chitin
- fructose-6-phosphate
-
glcn-6-phosphate
- non-o1
- drug development
- diagnostics
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetylglucosamine-6-phosphate deacetylase, glcnac-6-phosphate deacetylase, n-acetylglucosamine 6-phosphate deacetylase, lmo0956, n-acetylglucosamine-6-phosphate de-n-acetylase, lmo2108, msnaga, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase
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-
-
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acetylaminodeoxyglucosephosphate acetylhydrolase
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-
-
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acetylglucosamine phosphate deacetylase
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-
-
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deacetylase, acetylglucosaminephosphate
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-
-
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GlcNAc 6-P deacetylase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
active site structure at the bottom of the alpha-domain cavity, catalytic mechanism
N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
sequential mechanism with ordered release of products and a slow isomerization of the enzyme-acetate complex
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N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
catalytic mechanism, enzyme-substrate interaction analysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
N-acetyl-D-glucosamine-6-phosphate amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9027-50-3
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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
N-acetyl-D-galactosamine 6-phosphate + H2O
D-galactosamine 6-phosphate + acetate
-
-
-
?
N-acetyl-D-glucosamine 6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
-
-
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
?
N-formyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + formate
-
-
-
?
N-thioacetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + thioacetate
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-
-
?
N-trifluoroacetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + trifluoroacetate
-
-
-
?
D-glucosamine 6-phosphate + acetate
N-acetyl-D-glucosamine 6-phosphate + H2O
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-
-
r
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
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-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
step in amino sugar catabolism
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-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
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-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
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-
-
-
ir
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
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-
-
-
r
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
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enzyme is involved in aminosugar catabolism
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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
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
step in amino sugar catabolism
-
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
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enzyme is involved in aminosugar catabolism
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn
Zn2+
zinc metalloenzyme, Zn2+ is bound to the enzyme, 1.4 Zn2+ per polypeptide chain, the metal binding site also binds a phosphate ion
Zn2+
-
1 equivalent of zinc bound at the Mbeta site, the enzyme contains a binuclear metal center at the active site
additional information
additional information
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
additional information
-
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methyl phosphonamidates inhibitor 1
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tetrahedral reaction intermediate analogues
N-acetyl-D-glucosamine 6-phosphate
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substrate inhibition at high concentrations
additional information
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
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additional information
-
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Mn
0.15
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Co
0.2
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Cd
0.23
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Fe
0.64
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Ni
0.2
N-thioacetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Cd
0.23
N-thioacetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Mn
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35
N-acetyl-D-glucosamine 6-phosphate
enzyme with 0.4 eqivalents of Zn per subunit bound
41
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Ni
58
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Fe
92
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Mn
96
N-acetyl-D-glucosamine 6-phosphate
enzyme with 1 equivalent of Zn per subunit bound
163
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Cd
177
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Co
11
N-thioacetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Mn
128
N-thioacetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Cd
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000034
methyl phosphonamidates inhibitor 1
-
pH 7.5, 30°C, recombinant enzyme
additional information
additional information
-
inhibition kinetics, inhibitor binding model
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
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pH 7.0: about 45% of maximal activity, pH 9.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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part of the pathway responsible for the recycling of amino sugar components of peptidoglycan, the cataboloc pathway for the use of N-acetylglucosamine
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
analysis of the dimer-dimer interface, the tertiary and quarternary structure, the apoenzyme shows conformational changes in two loops adjacent to the active site, crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 18°C, precipitant is sodium dihydrogen phosphate, X-ray diffraction structure determination and analysis at 2.0-2.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a nagA mutation causes the accumulation of the allosteric activator GlcNAc6P, permitting allosteric activation of nagB, the GlcNAc6P deaminase, and derepresses the nag operon, with a stronger effect than a mutation of nagC, structure of the nag operon, overview
additional information
-
mutations in nagA result in accumulation of millimolar of N-acetylglucosamine, presumably by preventing peptidoglycan recycling. Mutations in the genes encoding the key enzymes upstream of nagA in the recycling pathway (amG, nagZ, nagK, murQ, and anmK), which are expected to interrupt the recycling process, reduce but do not eliminate accumulation of N-acetyl-6-phosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged dialysis against 10 mM sodium phosphate buffer, pH 7.0, causes little loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
Escherichia coli (P0AF18), Escherichia coli, Thermotoga maritima
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