Information on EC 3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.1.25
-
RECOMMENDED NAME
GeneOntology No.
N-acetylglucosamine-6-phosphate deacetylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
anhydromuropeptides recycling
-
-
Biosynthesis of antibiotics
-
-
chitin derivatives degradation
-
-
D-galactosamine and N-acetyl-D-galactosamine degradation
-
-
Galactose metabolism
-
-
N-acetyl-D-galactosamine degradation
-
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N-acetylglucosamine degradation I
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metabolism of amino sugars and derivatives
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-
SYSTEMATIC NAME
IUBMB Comments
N-acetyl-D-glucosamine-6-phosphate amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-50-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
var. pennsylvanicus
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
overproducing strain
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
formally known as Acetobacter xylinum
UniProt
Manually annotated by BRENDA team
formally known as Acetobacter xylinum
UniProt
Manually annotated by BRENDA team
several strains
-
-
Manually annotated by BRENDA team
Non-O1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucosamine 6-phosphate + acetate
N-acetyl-D-glucosamine 6-phosphate + H2O
show the reaction diagram
N-acetyl-D-galactosamine 6-phosphate + H2O
D-galactosamine 6-phosphate + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
show the reaction diagram
N-acetyl-D-glucosamine 6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
show the reaction diagram
N-acetyl-D-glucosamine-6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
show the reaction diagram
N-acetylglucosamine + H2O
D-glucosamine + acetate
show the reaction diagram
N-formyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + formate
show the reaction diagram
-
-
-
-
?
N-thioacetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + thioacetate
show the reaction diagram
-
-
-
-
?
N-trifluoroacetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + trifluoroacetate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
show the reaction diagram
N-acetyl-D-glucosamine-6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2-mercaptoethanol
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-
5,5'-dithio-bis(2-nitrobenzoate)
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-
acetate
Co2+
-
above 5 mM
fructose 1,6-diphosphate
-
72% inhibition at 0.2 mM and 90% inhibition at 0.7 mM
fructose-6-phosphate
glucosamine 6-phosphate
glucose 6-phosphate
iodoacetate
-
-
methyl phosphonamidates inhibitor 1
-
tetrahedral reaction intermediate analogues
N-acetyl-D-glucosamine 6-phosphate
-
substrate inhibition at high concentrations
N-methylhydroxyphosphinyl-D-glucosamine 6-phosphate
-
-
NEM
-
1 mM, complete inhibition
PCMB
-
0.1 mM, complete inhibition
UDP-N-acetylglucosamine
-
10 mM, 35% inhibition
UTP
-
7.5 mM, 21% inhibition
additional information
-
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
acetate
-
-
25
glucosamine 6-phosphate
-
-
1.24
N-Acetyl-D-galactosamine 6-phosphate
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-
0.04 - 3.6
N-acetyl-D-glucosamine 6-phosphate
4.9 - 11
N-acetyl-D-glucosamine 6-sulfate
73 - 120
N-acetylglucosamine
0.029 - 0.38
N-acetylglucosamine 6-phosphate
4.6 - 12
N-acetylglucosamine 6-sulfate
0.29
N-formyl-D-glucosamine 6-phosphate
-
-
0.2 - 0.24
N-thioacetyl-D-glucosamine 6-phosphate
0.4
N-trifluoroacetyl-D-glucosamine 6-phosphate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
154
N-Acetyl-D-galactosamine 6-phosphate
Escherichia coli
-
-
0.02 - 177
N-acetyl-D-glucosamine 6-phosphate
23 - 64
N-acetyl-D-glucosamine 6-sulfate
0.013 - 25
N-acetylglucosamine
0.12 - 0.97
N-acetylglucosamine 6-phosphate
0.074 - 50
N-acetylglucosamine 6-sulfate
22
N-formyl-D-glucosamine 6-phosphate
Escherichia coli
-
-
10 - 128
N-thioacetyl-D-glucosamine 6-phosphate
2610
N-trifluoroacetyl-D-glucosamine 6-phosphate
Escherichia coli
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000034
methyl phosphonamidates inhibitor 1
-
pH 7.5, 30°C, recombinant enzyme
additional information
additional information
-
inhibition kinetics, inhibitor binding model
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.5
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
-
more than 90% of maximal activity below pH 9.5 and above pH 7.0
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 hide
LITERATURE
45
-
hydrolysis of N-acetylglucosamine
55
-
hydrolysis of N-acetylglucosamine 6-phosphate
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
about 40% of maximal activity at 20°C and at 60°C, hydrolysis of N-acetylglucosamine
40 - 70
-
40°C: about 50% of maximal activity, 65°C: 60% of maximal activity, 70°C: 14% of maximal activity, hydrolysis of N-acetylglucosamine 6-phosphate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
extreme low activity
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
4 * 41000, SDS-PAGE
41670
x * 41670, sequence calculation, x * 45498, recombinant His-tagged enzyme, mass spectrometry
45000
-
4 * 45000, SDS-PAGE
45498
x * 41670, sequence calculation, x * 45498, recombinant His-tagged enzyme, mass spectrometry
148000
-
gel filtration
160000 - 165000
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non-denaturing PAGE, gel filtration
164000
-
non-denaturing PAGE
190000
-
gel filtration
345000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
crystallization data
homotetramer
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determined by gel filtration chromatography, SAXS and analytical ultracentrifugation, dimer of dimers
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
30 min, stable up to 29°C, enzyme retains more than 70% of its activity at 30°C, complete loss of activity at 45°C
246595
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
30 min, stable up to
29
-
pH 6.0-8.0, 30 min, stable up to
30
-
pH 6.0-8.0, 30 min, enzyme retains more than 70% of its activity
45
-
pH 6.0-8.0, 30 min, complete loss of activity
60
-
30 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged dialysis against 10 mM sodium phosphate buffer, pH 7.0, causes little loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Tris-HCl, pH 7.5, 25% glycerol, 2 mM CHAPS, stable for at least 2 months
-
4°C, 100 mM Tris/HCl, pH 7.2, stable for 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion exchange column
-
recombinant His-tagged enzyme from Escherichia coli strain C43(DE3) by nickel affinity chromatography and dialysis
size exclusion column and anion exchange column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Top10 cells
expression in Escherichia coli
-
gene lmo0956, genetic organization, phylogenetic analysis; gene lmo2108, genetic organization, phylogenetic analysis
NAG genes are expressed in Saccharomyces cerevisiae BY strains to study their effect on making novel carbon sources available for Saccharomyces cerevisiae
Q59RW2
recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain C43(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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