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alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
additional information
?
-
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
specific for
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
active towards alpha-anomer, inactive towards the beta-anomer. Strong affinity for the open-chain form of glucosamine 6-phosphate
-
?
additional information
?
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview
-
-
-
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GlcNAc6P
enzyme NagB is allosterically activated by GlcNAc6P
N-acetylglucosamine 6-phosphate
N-acetylglucosamine 6-phosphate
N-acetylglucosamine-6-phosphate
-
allosteric activator of NagB
N-acetylglucosamine 6-phosphate
-
N-acetylglucosamine 6-phosphate
-
-
N-acetylglucosamine 6-phosphate
-
-
N-acetylglucosamine 6-phosphate
-
activates
N-acetylglucosamine 6-phosphate
-
increases reaction velocity when D-glucosamine 6-phosphate is present at levels below that required for saturation
additional information
NanE, GlcNAc-6P epimerase, and the uridylylated PII protein allosterically activate NagB by direct protein-protein interactions, overview. Uridylylated PII (but not underivatized PII) activates NagB about 10fold at low concentrations of substrate, whereas NanE increases NagB activity about 2fold. NanE activates NagB in the absence or presence of GlcNAc-6P, but histidine-phosphorylatable phosphocarrier protein (HPr) and U-PII activation requires the presence of GlcNAc-6P. NanE-dependent activation of NagB is not dependent on GlcNAc-6P. Activation of NagB by HPr and uridylylated PII, as well as by NanE and HPr (but not by NanE and U-PII), is synergistic, and the modeling, which suggests specific residues involved in complex formation, provides possible explanations. The uridylylated PII protein (U-PII) is generated by posttranslational modification under nitrogen-limiting conditions involving the glutamine/2-oxoglutarate ratio-sensing uridylyltransferase/uridylyl-removing enzyme GlnD. PII (GlnB)-dependent activation of NagB depends on the uridylylation state of GlnB, kinetics for NagB in the presence of PII at different stages of PII modification involving uridylylation by GlnD, overview. The effect is greater at pH 7.5 than at pH 8 due to the allosteric behavior of the Ser-1 mutant NagB, resulting from an increased Hill coefficient, also noticed for the wild-type NagB. Modeling of HPr/U-PII and of HPr/NanE binding to NagB. The PII protein is known to be a regulator of both the activity and the synthesis of glutamine synthetase (GlnA) in enteric bacteria, and of nitrogen metabolism in many other bacteria, archaea, and eukaryotes, in response to the availability of nitrogen sources
-
additional information
-
enzyme contains 5 half-cystines per monomer, the sulfhydryls are not essential for catalysis or allosteric behavior of the enzyme
-
additional information
-
each subunit has for Cys residues located at positions 118, 219, 228 and 239, Cys118 and Cys239 form a pair of vicinal thiols
-
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0.85 - 3.6
alpha-D-glucosamine 6-phosphate
0.26 - 5.2
D-glucosamine 6-phosphate
1.7
D-fructose 6-phosphate
-
pH 7.7, 30°C, in presence of 0.5 mM N-acetylglucosamine 6-phosphate
0.4 - 9
D-glucosamine 6-phosphate
additional information
additional information
-
0.85
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
1.9
alpha-D-glucosamine 6-phosphate
pH 6.8, 30°C, 0.2 mM GlcNAc-6P, enzyme in absence of NanE
2
alpha-D-glucosamine 6-phosphate
pH 6.8, 30°C, 0.2 mM GlcNAc-6P, enzyme in presence of NanE
2.3
alpha-D-glucosamine 6-phosphate
pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in presence of PII protein
2.9
alpha-D-glucosamine 6-phosphate
pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in absence of PII protein
3.6
alpha-D-glucosamine 6-phosphate
pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in presence of uridylylated PII protein
0.26
D-glucosamine 6-phosphate
mutant W15Y/W224Y/Y254W, pH 7.5, S0.5-value 0.5 mM
0.33
D-glucosamine 6-phosphate
mutant R172A/K208E, Michaelis-Hill equation
0.46
D-glucosamine 6-phosphate
mutant C118S/C228S/C239S, pH 7.5, 30°C
0.49
D-glucosamine 6-phosphate
mutant W15Y/F174W/W224Y, pH 7.5, S0.5-value 3.4 mM
0.49
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C206, pH 7.5, 30°C
0.5
D-glucosamine 6-phosphate
mutant W224Y, pH 7.5, S0.5-value 4.8 mM
0.5
D-glucosamine 6-phosphate
wild-type, pH 7.5, 30°C
0.51
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C
0.52
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C
0.52
D-glucosamine 6-phosphate
wild-type, modified with bimane at C206, pH 7.5, 30°C
0.55
D-glucosamine 6-phosphate
wild-type, Michaelis-Hill equation
0.55
D-glucosamine 6-phosphate
wild-type, pH 7.5, S0.5-value 5.5 mM
0.61
D-glucosamine 6-phosphate
mutant K208E, Michaelis-Hill equation
0.62
D-glucosamine 6-phosphate
mutant W15Y, pH 7.5, S0.5-value 5.8 mM
0.65
D-glucosamine 6-phosphate
mutant W15Y/W224Y, pH 7.5, S0.5-value 5.0 mM
0.69
D-glucosamine 6-phosphate
mutant K208V, Michaelis-Hill equation
1.67
D-glucosamine 6-phosphate
mutant R172A, Michaelis-Hill equation
4.6
D-glucosamine 6-phosphate
wild-type, modified with bimane at C206, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.1
D-glucosamine 6-phosphate
mutant C118S/C228S/C239S, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.1
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.1
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C206, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.2
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.2
D-glucosamine 6-phosphate
wild-type, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
0.4
D-glucosamine 6-phosphate
-
pH 7.8, 25°C
0.55
D-glucosamine 6-phosphate
-
pH 7.5, 30°C, wild-type enzyme, in presence of N-acetylglucosamine 6-phosphate
0.67
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, mutant enzyme Tyr121Trp
1.2
D-glucosamine 6-phosphate
-
pH 7.8, 37°C, activated by N-acetylglucosamine 6-phosphate
2.01
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, wild-type enzyme
2.2
D-glucosamine 6-phosphate
-
in presence of 0.2 mM N-acetylglucosamine 6-phosphate
2.6
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, mutant enzyme Tyr121Thr
3.43
D-glucosamine 6-phosphate
-
pH 7.5, 30°C, mutant F174A, in presence of N-acetylglucosamine 6-phosphate
7.1
D-glucosamine 6-phosphate
-
pH 7.8, 37°C
9
D-glucosamine 6-phosphate
-
pH 7.5, 37°C
31.4
NH4+
-
pH 7.7, 30°C, in presence of 0.25 mM N-acetylglucosamine 6-phosphate
35.4
NH4+
-
pH 7.7, 30°C, without activator
additional information
additional information
comparison of KM of unmodified and N-terminal modified enzyme
-
additional information
additional information
-
comparison of KM of unmodified and N-terminal modified enzyme
-
additional information
additional information
comparison of KM of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
-
comparison of KM of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
steady-state kinetics of NagB in presence or absence of activators, overview
-
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107 - 220
alpha-D-glucosamine 6-phosphate
0.044 - 160
D-glucosamine 6-phosphate
455
D-fructose 6-phosphate
-
pH 7.7, 30°C
11.4 - 1800
D-glucosamine 6-phosphate
additional information
additional information
-
107
alpha-D-glucosamine 6-phosphate
mutant C118Ser/C228S/C239S/D165C/S206W, at pH 7.8 and 30°C
158
alpha-D-glucosamine 6-phosphate
wild type enzyme, at pH 7.8 and 30°C
220
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
0.044
D-glucosamine 6-phosphate
mutant K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
2
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C
6.1
D-glucosamine 6-phosphate
mutant R172A/K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
7.8
D-glucosamine 6-phosphate
mutant K208V, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
11.8
D-glucosamine 6-phosphate
mutant R172A, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
26.7
D-glucosamine 6-phosphate
mutant W15Y/W224Y/Y254W, pH 7.5
69.5
D-glucosamine 6-phosphate
wild-type, modified with bimane at C206, pH 7.5, 30°C
70.6
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C
70.9
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C206, pH 7.5, 30°C
71.6
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C
80
D-glucosamine 6-phosphate
mutant W15Y/F174W/W224Y, pH 7.5
96
D-glucosamine 6-phosphate
mutant C118S/C228S/C239S, pH 7.5, 30°C
134
D-glucosamine 6-phosphate
mutant W15Y, pH 7.5
138
D-glucosamine 6-phosphate
mutant W224Y, pH 7.5
144
D-glucosamine 6-phosphate
mutant W15Y/W224Y, pH 7.5
153
D-glucosamine 6-phosphate
wild-type, pH 7.5, 30°C
158
D-glucosamine 6-phosphate
wild-type, pH 7.5
160
D-glucosamine 6-phosphate
wild-type, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
11.4
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254F
75
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254F in presence of N-acetylglucosamine 6-phosphate
218
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254T
248
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254T in presence of N-acetylglucosamine 6-phosphate
292
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, wild-type enzyme
320
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, wild-type enzyme in presence of N-acetylglucosamine 6-phosphate
1800
D-glucosamine 6-phosphate
-
pH 7.7, 30°C
additional information
additional information
comparison of kcat of unmodified and N-terminal modified enzyme
-
additional information
additional information
-
comparison of kcat of unmodified and N-terminal modified enzyme
-
additional information
additional information
comparison of kcat of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
-
comparison of kcat of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
-
-
-
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C118S/C228S/C239S
decrease in kcat-value, no modification of allosteric activation
C118Ser/C228S/C239S/D165C/S206W
the mutant shows reduced turnover number compared to the wild type enzyme
D141N
the mutation modifies the kcat versus pH profile of the enzyme
D141N/E148Q
mutation modifies the kcat versus pH profile of the enzyme
E148Q
the mutation modifies the kcat versus pH profile of the enzyme
H143Q
drastically impairs the activity of the enzyme in the forward but not in the backward direction of the reaction
K208E
entirely inactive in absence of allosteric activator N-acetylglucose-6-phosphate
K208V
homotropic cooperativity, Hill-coefficient 1.7, 2fold increase in dissociation constant for allosteric activator N-acetylglucose-6-phosphate compared to wild-type
R172A
inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant
R172A/K208E
inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant
W15Y
mutant containing a single Trp residue at W224
W15Y/F174W/W224Y
mutant containing a single, new Trp-residue at F174W
W15Y/W224Y
mutant without Trp residues
W15Y/W224Y/Y254W
mutant containing a single, new Trp-residue at Y254W
W224Y
mutant containing a single Trp residue at W15
C219S
-
the kinetic and allosteric properties of the mutant enzyme in which Ser replaces Cys219 or Cys228 are the same as those described for the wild-type enzyme. The same result is obtained with the double mutation
C228S
-
the kinetic and allosteric properties of the mutant enzyme in which Ser replaces Cys219 or Cys228 are the same as those described for the wild-type enzyme. The same result is obtained with the double mutation
Y121T
-
while the wild-type enzyme behaves as a classical allosteric K-system which can be described by the allosteric concerted model, the mutant forms Y121T and Y121W present an asymmetric behaviour towards the allosteric activator, which can be described as two distinct half-of-the-sites allosteric activation steps occuring with different affinities for the N-acetyl-D-glucosamine 6-phosphate
Y121W
-
while the wild-type enzyme behaves as a classical allosteric K-system which can be described by the allosteric concerted model, the mutant forms Y121T and Y121W present an asymmetric behaviour towards the allosteric activator, which can be described as two distinct half-of-the-sites allosteric activation steps occuring with different affinities for the N-acetyl-D-glucosamine 6-phosphate
Y254F
-
the mutant is less active than wild-type enzyme, the replacement causes an uncoupling of the homotropic and heterotrophic effects
Y254T
-
the mutation results in pure K-system with a similar catalytic activity to that of the wild-type enzyme, mutant displays kcat values similar to the wild-type enzyme
F174A
-
the mutation effectively weakens the interaction between the active-site lid and the rest of the enzyme molecule, the mutant is essentially inactive in the absence of its allosteric activator
F174A
-
the mutant requires higher concentrations of N-acetylglucosamine-6-phosphate for activity in vitro. The mutant strain grows better on glucosamine in the presence of N-acetylglucosamine-6-phosphate
additional information
construction of bacterial strains LAA199 (nagBEc+) and LAA195 (nagBBs+). The gene for the Escherichia coli allosteric NagBEc enzyme is replaced with that of the nonallosteric Bacillus subtilis homologue NagBBs. No effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB. Deletion of the nagB gene had no strong effect on the amino sugar pools
additional information
-
construction of bacterial strains LAA199 (nagBEc+) and LAA195 (nagBBs+). The gene for the Escherichia coli allosteric NagBEc enzyme is replaced with that of the nonallosteric Bacillus subtilis homologue NagBBs. No effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB. Deletion of the nagB gene had no strong effect on the amino sugar pools
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Comb, D.G.; Roseman, S.
Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase
J. Biol. Chem.
232
807-827
1958
Escherichia coli, Sus scrofa
brenda
Withe, R.J.; Pasternak, Ch.A.
N-Acetylglucosamine-6-phosphate deacetylase and glucosamine-6-phosphate deaminase from Escherichia coli
Methods Enzymol.
41B
497-502
1975
Escherichia coli
brenda
Midelfort, C.F.; Rose, I.A.
Studies on the mechanism of Escherichia coli glucosamine-6-phosphate isomerase
Biochemistry
16
1590-1596
1977
Escherichia coli
brenda
Calcagno, M.; Campos, P.J.; Mulliert, G.; Suastegui, J.
Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from Escherichia coli
Biochim. Biophys. Acta
787
165-173
1984
Escherichia coli
brenda
Altamirano, M.M.; Mulliert, G.; Calcagno, M.
Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli
Arch. Biochem. Biophys.
253
95-100
1987
Escherichia coli
brenda
Oliva, G.; Fontes, M.R.; Garratt, R.C.; Altamirano, M.M.; Calcagno, M.L.; Horjales, E.
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution
Structure
3
1323-1332
1995
Escherichia coli
brenda
Altamirano, M.M.; Plumbridge, J.A.; Barba, H.A.; Calcagno, M.L.
Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides
Biochem. J.
295
645-648
1993
Escherichia coli
brenda
Altamirano, M.M.; Plumbridge, J.A.; Horjales, H.; Calcagno, M.L.
Asymmetric allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase produced by replacement of Tyr121
Biochemistry
34
6074-6082
1995
Escherichia coli
brenda
Altamirano, M.M.; Calcagno, M.
Zinc binding and its trapping by allosteric transition in glucosamine-6-phosphate deaminase from Escherichia coli
Biochim. Biophys. Acta
1038
291-294
1990
Escherichia coli
brenda
Horjales, E.; Altamirano, M.M.; Calcagno, M.L.; Dauter, Z.; Wilson, K.; Garratt, R.C.; Oliva, G.
Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12
J. Mol. Biol.
226
1283-1286
1992
Escherichia coli
brenda
Montero-Moran, G.M.; Horjales, E.; Calcagno, M.L.; Altamirano, M.M.
Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotrophic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase
Biochemistry
37
7844-7849
1998
Escherichia coli
brenda
Lara-Gonzalez, S.; Dixon, H.B.; Mendoza-Hernandez, G.; Altamirano, M.M.; Calcagno, M.L.
On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli
J. Mol. Biol.
301
219-227
2000
Escherichia coli (P0A759), Escherichia coli
brenda
Montero-Moran, G.M.; Lara-Gonzalez, S.; Alvarez-Anorve, L.I.; Plumbridge, J.A.; Calcagno, M.L.
On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase
Biochemistry
40
10187-10196
2001
Escherichia coli (P0A759), Escherichia coli
brenda
Rudino-Pinera, E.; Morales-Arrieta, S.; Rojas-Trejo, S.P.; Horjales, E.
Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase
Acta Crystallogr. Sect. D
58
10-20
2002
Escherichia coli (P0A759), Escherichia coli
brenda
Bustos-Jaimes, I.; Calcagno, M.L.
Allosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli
Arch. Biochem. Biophys.
394
156-160
2001
Escherichia coli
brenda
Bustos-Jaimes, I.; Sosa-Peinado, A.; Rudino-Pinera, E.; Horjales, E.; Calcagno, M.L.
On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase
J. Mol. Biol.
319
183-189
2002
Escherichia coli
brenda
Lucumi-Moreno, A.; Calcagno, M.L.
On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase
Arch. Biochem. Biophys.
442
41-48
2005
Escherichia coli (P0A759), Escherichia coli
brenda
Bustos-Jaimes, I.; Ramirez-Costa, M.; De Anda-Aguilar, L.; Hinojosa-Ocana, P.; Calcagno, M.L.
Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase
Biochemistry
44
1127-1135
2005
Escherichia coli (P0A759), Escherichia coli
brenda
Sosa-Peinado, A.; Gonzalez-Andrade, M.
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate deaminase of Escherichia coli induced by active or allosteric site ligands at steady state
Biochemistry
44
15083-15092
2005
Escherichia coli (P0A759), Escherichia coli
brenda
Alvarez-Anorve, L.I.; Bustos-Jaimes, I.; Calcagno, M.L.; Plumbridge, J.
Allosteric regulation of glucosamine-6-phosphate deaminase (NagB) and growth of Escherichia coli on glucosamine
J. Bacteriol.
191
6401-6407
2009
Escherichia coli
brenda
Zonszein, S.; Alvarez-Anorve, L.I.; Vazquez-Nunez, R.J.; Calcagno, M.L.
The tertiary origin of the allosteric activation of E. coli glucosamine-6-phosphate deaminase studied by sol-gel nanoencapsulation of its T conformer
PLoS ONE
9
e96536
2014
Escherichia coli (P0A759), Escherichia coli
brenda
Alvarez-Anorve, L.I.; Gaugue, I.; Link, H.; Marcos-Viquez, J.; Diaz-Jimenez, D.M.; Zonszein, S.; Bustos-Jaimes, I.; Schmitz-Afonso, I.; Calcagno, M.L.; Plumbridge, J.
Allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase (NagB) in vivo justified by intracellular amino sugar metabolite concentrations
J. Bacteriol.
198
1610-1620
2016
Bacillus subtilis (O35000), Bacillus subtilis, Bacillus subtilis 168 (O35000), Escherichia coli (P0A759), Escherichia coli
brenda
Rodionova, I.A.; Goodacre, N.; Babu, M.; Emili, A.; Uetz, P.; Saier, M.H.
The nitrogen regulatory PII protein (GlnB) and N-acetylglucosamine 6-phosphate epimerase (NanE) allosterically activate glucosamine 6-phosphate deaminase (NagB) in Escherichia coli
J. Bacteriol.
200
e00691_17
2018
Escherichia coli (P0A759)
brenda