Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-glucosamine 6-phosphate + acetate
N-acetyl-D-glucosamine 6-phosphate + H2O
N-acetyl-D-galactosamine 6-phosphate + H2O
D-galactosamine 6-phosphate + acetate
-
-
-
?
N-acetyl-D-galactosamine-6-phosphate + H2O
D-galactosamine 6-phosphate + acetate
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 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-acetyl-D-glucosamine-6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
N-acetyl-D-mannosamine-6-phosphate + H2O
D-mannosamine 6-phosphate + acetate
N-acetylglucosamine + H2O
D-glucosamine + 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
-
-
-
?
N-trifluoroacetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + trifluoroacetate
-
-
-
?
additional information
?
-
D-glucosamine 6-phosphate + acetate
N-acetyl-D-glucosamine 6-phosphate + H2O
-
-
-
r
D-glucosamine 6-phosphate + acetate
N-acetyl-D-glucosamine 6-phosphate + H2O
-
-
-
r
N-acetyl-D-galactosamine-6-phosphate + H2O
D-galactosamine 6-phosphate + acetate
very low activity
-
-
?
N-acetyl-D-galactosamine-6-phosphate + H2O
D-galactosamine 6-phosphate + acetate
low activity
-
-
?
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
-
-
-
-
?
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
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
enzyme of the N-acetylglucosamine pathway
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
enzyme of the N-acetylglucosamine pathway
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
inducible enzyme, trichodermin and lomofungin inhibit induction of the enzyme
-
?
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
-
-
-
-
ir
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
-
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
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
enzyme is involved in aminosugar catabolism
-
-
?
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
-
-
-
-
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
-
pathway of N-acetylglucosamine metabolism
-
-
?
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
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
pathway of N-acetylglucosamine metabolism
-
-
?
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
-
presence of high deacetylase activity in endothelial cells and Kupffer cells but a virtual lack of activity in hepatocytes, suggests that the major part of the N-acetylglucosamine generated by the catabolism of glycoconjugates in the latter cells is reused in the synthesis of new complex carbohydrate molecules
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
Vibrio cholerae serotype O1 Non-O1
-
-
-
-
?
N-acetyl-D-glucosamine 6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
-
-
-
?
N-acetyl-D-glucosamine 6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
Vibrio cholerae serotype O1 Non-O1
-
-
-
-
?
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
preferred substrate
-
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
preferred substrate, structure of the GlcNAc6P substrate-binding site in MSNagA, overview
-
-
?
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
-
-
-
-
?
N-acetyl-D-glucosamine-6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
-
-
-
?
N-acetyl-D-glucosamine-6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
low activity
-
-
?
N-acetyl-D-glucosamine-6-sulfate + H2O
D-glucosamine 6-sulfate + acetate
-
-
-
?
N-acetyl-D-mannosamine-6-phosphate + H2O
D-mannosamine 6-phosphate + acetate
low activity
-
-
?
N-acetyl-D-mannosamine-6-phosphate + H2O
D-mannosamine 6-phosphate + acetate
low activity
-
-
?
N-acetylglucosamine + H2O
D-glucosamine + acetate
-
-
-
-
?
N-acetylglucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetylglucosamine + H2O
D-glucosamine + acetate
-
-
-
-
?
N-acetylglucosamine + H2O
D-glucosamine + acetate
Vibrio cholerae serotype O1 Non-O1
-
-
-
?
additional information
?
-
no catalytic activity toward GlcNAc, GlcNGc6P, and MurNAc6P
-
-
?
additional information
?
-
-
no catalytic activity toward GlcNAc, GlcNGc6P, and MurNAc6P
-
-
?
additional information
?
-
no catalytic activity toward N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
no catalytic activity toward N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
performance of a coupled assay with NagB (EC 3.5.99.6) resulting in production of fructose 6-phosphate and NH3
-
-
?
additional information
?
-
-
performance of a coupled assay with NagB (EC 3.5.99.6) resulting in production of fructose 6-phosphate and NH3
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
enzyme of the N-acetylglucosamine pathway
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
enzyme of the N-acetylglucosamine pathway
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
inducible enzyme, trichodermin and lomofungin inhibit induction of the enzyme
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
enzyme is involved in aminosugar catabolism
-
-
?
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
-
pathway of N-acetylglucosamine metabolism
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
pathway of N-acetylglucosamine metabolism
-
-
?
N-acetyl-D-glucosamine 6-phosphate + H2O
D-glucosamine 6-phosphate + acetate
-
presence of high deacetylase activity in endothelial cells and Kupffer cells but a virtual lack of activity in hepatocytes, suggests that the major part of the N-acetylglucosamine generated by the catabolism of glycoconjugates in the latter cells is reused in the synthesis of new complex carbohydrate molecules
-
-
?
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
-
-
-
?
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
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
25
glucosamine 6-phosphate
-
-
1.24
N-Acetyl-D-galactosamine 6-phosphate
-
118.5 - 145.4
N-acetyl-D-galactosamine-6-phosphate
0.04 - 3.6
N-acetyl-D-glucosamine 6-phosphate
4.9 - 11
N-acetyl-D-glucosamine 6-sulfate
0.16 - 5.2
N-acetyl-D-glucosamine-6-phosphate
20.9 - 21.4
N-acetyl-D-glucosamine-6-sulfate
19.1 - 19.3
N-acetyl-D-mannosamine-6-phosphate
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
-
additional information
additional information
-
118.5
N-acetyl-D-galactosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
145.4
N-acetyl-D-galactosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged enzyme
0.04
N-acetyl-D-glucosamine 6-phosphate
-
-
0.08
N-acetyl-D-glucosamine 6-phosphate
-
0.08
N-acetyl-D-glucosamine 6-phosphate
mutant Q59A
0.1
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Mn
0.15
N-acetyl-D-glucosamine 6-phosphate
mutant E131A
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
0.3
N-acetyl-D-glucosamine 6-phosphate
-
-
0.3
N-acetyl-D-glucosamine 6-phosphate
-
-
0.3
N-acetyl-D-glucosamine 6-phosphate
-
at 10°C
0.31
N-acetyl-D-glucosamine 6-phosphate
mutant Q59H
0.33
N-acetyl-D-glucosamine 6-phosphate
mutant H143Q
0.4
N-acetyl-D-glucosamine 6-phosphate
-
-
0.64
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Ni
0.76
N-acetyl-D-glucosamine 6-phosphate
mutant Y223F
0.8
N-acetyl-D-glucosamine 6-phosphate
-
-
0.8
N-acetyl-D-glucosamine 6-phosphate
mutant N61A
1
N-acetyl-D-glucosamine 6-phosphate
-
-
1.7
N-acetyl-D-glucosamine 6-phosphate
mutant N61H
2
N-acetyl-D-glucosamine 6-phosphate
mutant K139M
2.1
N-acetyl-D-glucosamine 6-phosphate
mutant H143N
2.7
N-acetyl-D-glucosamine 6-phosphate
mutant H251N
3.6
N-acetyl-D-glucosamine 6-phosphate
mutant E131Q
4.9
N-acetyl-D-glucosamine 6-sulfate
-
11
N-acetyl-D-glucosamine 6-sulfate
Zn in acitve site changed to Cd
0.16
N-acetyl-D-glucosamine-6-phosphate
-
pH 8.0, 30°C, recombinant enzyme
3
N-acetyl-D-glucosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged enzyme
3.2
N-acetyl-D-glucosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
5.2
N-acetyl-D-glucosamine-6-phosphate
pH 7.0, 37°C, recombinant wild-type His6-tagged enzyme expressed from Escherichia coli
20.9
N-acetyl-D-glucosamine-6-sulfate
pH 7.0, 37°C, recombinant His6-tagged enzyme
21.4
N-acetyl-D-glucosamine-6-sulfate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
19.1
N-acetyl-D-mannosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
19.3
N-acetyl-D-mannosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged enzyme
73
N-acetylglucosamine
-
-
98
N-acetylglucosamine
-
at 10°C
120
N-acetylglucosamine
-
at 30°C
0.029
N-acetylglucosamine 6-phosphate
-
-
0.03
N-acetylglucosamine 6-phosphate
-
-
0.38
N-acetylglucosamine 6-phosphate
-
at 30°C
4.6
N-acetylglucosamine 6-sulfate
-
-
5.9
N-acetylglucosamine 6-sulfate
-
at 10°C
12
N-acetylglucosamine 6-sulfate
-
at 30°C
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
0.24
N-thioacetyl-D-glucosamine 6-phosphate
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Mente kinetics. The initial rate measured for NagA has a significant substrate concentration-dependent lag phase which is not influenced by 1 mM Zn2+ and not pH-dependent
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
154
N-Acetyl-D-galactosamine 6-phosphate
-
5.4 - 31.1
N-acetyl-D-galactosamine-6-phosphate
0.02 - 177
N-acetyl-D-glucosamine 6-phosphate
23 - 64
N-acetyl-D-glucosamine 6-sulfate
20.7 - 345
N-acetyl-D-glucosamine-6-phosphate
3 - 33.2
N-acetyl-D-glucosamine-6-sulfate
18.2 - 70.6
N-acetyl-D-mannosamine-6-phosphate
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
-
10 - 128
N-thioacetyl-D-glucosamine 6-phosphate
2610
N-trifluoroacetyl-D-glucosamine 6-phosphate
-
5.4
N-acetyl-D-galactosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged enzyme
31.1
N-acetyl-D-galactosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
0.02
N-acetyl-D-glucosamine 6-phosphate
mutant D273A
0.02
N-acetyl-D-glucosamine 6-phosphate
mutant D273N
0.43
N-acetyl-D-glucosamine 6-phosphate
mutant H143N
0.7
N-acetyl-D-glucosamine 6-phosphate
mutant E131Q
1.9
N-acetyl-D-glucosamine 6-phosphate
mutant E131A
2.4
N-acetyl-D-glucosamine 6-phosphate
mutant H143Q
2.6
N-acetyl-D-glucosamine 6-phosphate
mutant N61H
6.8
N-acetyl-D-glucosamine 6-phosphate
mutant H251N
10
N-acetyl-D-glucosamine 6-phosphate
mutant Q59A
24
N-acetyl-D-glucosamine 6-phosphate
mutant N61A
32
N-acetyl-D-glucosamine 6-phosphate
mutant Q59H
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
49
N-acetyl-D-glucosamine 6-phosphate
mutant K139M
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
105
N-acetyl-D-glucosamine 6-phosphate
-
-
110
N-acetyl-D-glucosamine 6-phosphate
-
-
163
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Cd
167
N-acetyl-D-glucosamine 6-phosphate
mutant Y223F
177
N-acetyl-D-glucosamine 6-phosphate
Zn in acitve site changed to Co
23
N-acetyl-D-glucosamine 6-sulfate
Zn in acitve site changed to Cd
64
N-acetyl-D-glucosamine 6-sulfate
-
20.7
N-acetyl-D-glucosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Escherichia coli
36.8
N-acetyl-D-glucosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged enzyme
91.1
N-acetyl-D-glucosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
345
N-acetyl-D-glucosamine-6-phosphate
-
pH 8.0, 30°C, recombinant enzyme
3 - 6
N-acetyl-D-glucosamine-6-sulfate
pH 7.0, 37°C, recombinant His6-tagged enzyme
33.2
N-acetyl-D-glucosamine-6-sulfate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
18.2
N-acetyl-D-mannosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged enzyme
70.6
N-acetyl-D-mannosamine-6-phosphate
pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis
0.013
N-acetylglucosamine
-
at 10°C
0.63
N-acetylglucosamine
-
at 30°C
25
N-acetylglucosamine
-
-
0.12
N-acetylglucosamine 6-phosphate
-
at 10°C
0.68
N-acetylglucosamine 6-phosphate
-
at 30°C
0.97
N-acetylglucosamine 6-phosphate
-
-
0.074
N-acetylglucosamine 6-sulfate
-
at 30°C
0.34
N-acetylglucosamine 6-sulfate
-
at 30°C
50
N-acetylglucosamine 6-sulfate
-
-
10
N-thioacetyl-D-glucosamine 6-phosphate
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
mutants deficient in protein Lmo0956 reveal strikingly altered cell morphology, strongly reduced cell wall murein content and decreased sensitivity to cell wall hydrolase, mutanolysin and peptide antibiotic, colistin
malfunction
UDP-N-acetylglucosamine synthesis and bacterial growth (due to lack of N-acetylglucosamine utilization) is completely inhibited in N-acetylglucosamine 6-phosphate deacetylase disruption mutants
malfunction
-
UDP-N-acetylglucosamine synthesis and bacterial growth (due to lack of N-acetylglucosamine utilization) is completely inhibited in N-acetylglucosamine 6-phosphate deacetylase disruption mutants
-
metabolism
gene products of operon 150, consisting of three genes: lmo0956, lmo0957, and lmo0958, are necessary for the cytosolic steps of the amino-sugar-recycling pathway. The reverse reaction to Glc-N-6-P is catalyzed by GlmS
metabolism
-
N-acetylglucosamine-6-phosphate deacetylase (NagA) and glucosamine-6-phosphate deaminase (NagB) are branch point enzymes that direct amino sugars into different pathways
metabolism
the enzyme NagA catalyzes a metabolic step that connects the glycolysis pathway with the peptidoglycan biosynthesis and the synthesis of cell wall macromolecules, overview
metabolism
the enzyme NagA catalyzes a metabolic step that connects the glycolysis pathway with the peptidoglycan biosynthesis and the synthesis of cell wall macromolecules, overview
metabolism
-
N-acetylglucosamine-6-phosphate deacetylase (NagA) and glucosamine-6-phosphate deaminase (NagB) are branch point enzymes that direct amino sugars into different pathways
-
physiological function
-
part of the pathway responsible for the recycling of amino sugar components of peptidoglycan, the cataboloc pathway for the use of N-acetylglucosamine
physiological function
-
the Candida albicans genes encoding GlcNAc permease, GlcNAc kinase, GlcNAc-6-phosphate deacetylase, and glucosamine-6-phosphate deaminase are expressed in Saccharomyces cerevisiae strains to enable the use of GlcNAc as a carbon source. Chitin is the second abundant polysaccharide after cellulose and consists of N-acetylglucosamine moieties, which cannot be used by wild-type Saccharomyces cerevisiae
physiological function
Lmo0956 protein is required for cell wall peptidoglycan and teichoic acid biosynthesis and is essential for bacterial cell growth, cell division, and sensitivity to cell wall hydrolases and peptide antibiotics. Lmo0956 and Lmo2108 are involved in the deacetylation of muropeptides that have been taken up into the bacterial cell
physiological function
the enzyme plays an essential role for N-acetylglucosamine assimilation by Gluconacetobacter xylinus thus is required for the growth and survival for the bacterium in presence of N-acetylglucosamine as carbon source
physiological function
cytoplasmic de-N-acetylase Lmo0956 is required for cell wall peptidoglycan and teichoic acid biosynthesis and is also essential for bacterial cell growth, cell division, and sensitivity to cell wall hydrolases and peptide antibiotics
physiological function
-
part of the pathway responsible for the recycling of amino sugar components of peptidoglycan, the cataboloc pathway for the use of N-acetylglucosamine
-
physiological function
-
the Candida albicans genes encoding GlcNAc permease, GlcNAc kinase, GlcNAc-6-phosphate deacetylase, and glucosamine-6-phosphate deaminase are expressed in Saccharomyces cerevisiae strains to enable the use of GlcNAc as a carbon source. Chitin is the second abundant polysaccharide after cellulose and consists of N-acetylglucosamine moieties, which cannot be used by wild-type Saccharomyces cerevisiae
-
physiological function
-
the enzyme plays an essential role for N-acetylglucosamine assimilation by Gluconacetobacter xylinus thus is required for the growth and survival for the bacterium in presence of N-acetylglucosamine as carbon source
-
additional information
enzyme structure modeling, overview
additional information
enzyme structure modeling, overview
additional information
-
enzyme structure modeling, overview
additional information
-
involvement of both subunits in binding substrate by NagA. NagA requires two Zn2+ metal ions for activity and displays an unusual hysteretic behaviour, which may have a role in regulating flux at this step
additional information
the GlcNAc6P complex structure discloses the precise mode of GlcNAc6P binding and the structural framework of the active site, including two divalent metals located in the alpha/beta binuclear site. Enzyme structure comparisons, overview
additional information
-
the GlcNAc6P complex structure discloses the precise mode of GlcNAc6P binding and the structural framework of the active site, including two divalent metals located in the alpha/beta binuclear site. Enzyme structure comparisons, overview
additional information
-
involvement of both subunits in binding substrate by NagA. NagA requires two Zn2+ metal ions for activity and displays an unusual hysteretic behaviour, which may have a role in regulating flux at this step
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotetramer
-
determined by gel filtration chromatography, SAXS and analytical ultracentrifugation, dimer of dimers
?
x * 41670, sequence calculation, x * 45498, recombinant His-tagged enzyme, mass spectrometry
?
-
x * 41670, sequence calculation, x * 45498, recombinant His-tagged enzyme, mass spectrometry
-
dimer
-
crystallization data
dimer
-
NagA is an asymmetric dimer in solution, analytical ultracentrifugation and small-angle X-ray scattering data
dimer
-
NagA is an asymmetric dimer in solution, analytical ultracentrifugation and small-angle X-ray scattering data
-
tetramer
-
tetramer
-
4 * 41000, SDS-PAGE
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
tetramer
-
4 * 41000, SDS-PAGE
-
tetramer
-
4 * 45000, SDS-PAGE
tetramer
Vibrio cholerae serotype O1 Non-O1
-
4 * 45000, SDS-PAGE
-
additional information
enzyme structure comparisons, overview
additional information
-
enzyme structure comparisons, overview
additional information
-
involvement of both subunits in binding substrate
additional information
-
involvement of both subunits in binding substrate
-
additional information
the enzyme contains four internal disulfide bonds, Cys246, Cys256, Cys274, and Cys350 that may contribute to the formation of six internal disulfide bridges. Tryptic peptide mapping of the enzyme, overview
additional information
-
the enzyme contains four internal disulfide bonds, Cys246, Cys256, Cys274, and Cys350 that may contribute to the formation of six internal disulfide bridges. Tryptic peptide mapping of the enzyme, overview
additional information
-
the enzyme contains four internal disulfide bonds, Cys246, Cys256, Cys274, and Cys350 that may contribute to the formation of six internal disulfide bridges. Tryptic peptide mapping of the enzyme, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D272A
site-directed mutagenesis, inactive mutant
E127A
site-directed mutagenesis, inactive mutant
H139A
site-directed mutagenesis, inactive mutant
H249A
site-directed mutagenesis, inactive mutant
R225A
site-directed mutagenesis, inactive mutant
D267A
site-directed mutagenesis, inactive mutant
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
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
-
additional information
knockout of gene lmo0956, phenotype, overview
additional information
knockout of gene lmo0956, phenotype, overview
additional information
-
knockout of gene lmo0956, phenotype, overview
additional information
knockout of gene lmo1208, phenotype, overview
additional information
knockout of gene lmo1208, phenotype, overview
additional information
-
knockout of gene lmo1208, phenotype, overview
additional information
construction of mutant enzymes mutated to either a QXN motif to replicate the single metal-binding motif found in both the Escherichia coli and Vibrio cholerae NagA enzymes, or to AXA, resulting in highly reduced activity for the QXN mutant and complete loss of activity for the AXA mutant
additional information
-
construction of mutant enzymes mutated to either a QXN motif to replicate the single metal-binding motif found in both the Escherichia coli and Vibrio cholerae NagA enzymes, or to AXA, resulting in highly reduced activity for the QXN mutant and complete loss of activity for the AXA mutant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda