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Information on EC 3.5.99.6 - glucosamine-6-phosphate deaminase and Organism(s) Escherichia coli and UniProt Accession P0A759

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IUBMB Comments
The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
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Select one or more organisms in this record:
This record set is specific for:
Escherichia coli
UNIPROT: P0A759
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Escherichia coli
Synonyms
2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol-isomerizing), 2-amino-2-deoxy-D-glucose-6-phosphate ketol isomerase (deaminating), 5.3.1.10, aminodeoxyglucosephosphate isomerase, EC 5.3.1.10, GlcN-6-P isomerase, GlcN6P deaminase, glucosamine 6-phosphate deaminase, glucosamine 6-phosphate isomerase, glucosamine phosphate deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate ketol isomerase (deaminating)
-
-
-
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aminodeoxyglucosephosphate isomerase
-
-
-
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GlcN-6-P isomerase
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-
-
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GlcN6P deaminase
glucosamine 6-phosphate deaminase
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-
-
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glucosamine 6-phosphate isomerase
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-
-
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glucosamine phosphate deaminase
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-
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glucosamine-6-phosphate deaminase
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-
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glucosamine-6P deaminase
246
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glucosamine-P isomerase
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-
-
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glucosaminephosphate isomerase
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-
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GNPDA
isomerase, glucosamine phosphate
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-
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oscillin
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-
-
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phoshoglucosamine isomerase
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-
-
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phosphoglucosaminisomerase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-10-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
show the reaction diagram
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
show the reaction diagram
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
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-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
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-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,5-anhydro mannitol 6-phosphate
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2-deoxy-2-amino-D-glucitol 6-phosphate
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5,5'-dithiobis(2-nitrobenzoate)
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D-fructose 6-phosphate
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D-fructose oxime 6-phosphate
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diethyl dicarbonate
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complete inactivation, 2-deoxy-2-amino-D-glucitol 6-phosphate protects
Zn2+
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tightly bound and slow partial inhibitor
additional information
-
not: alpha and beta O-methyl glycoside of D-fructose 6-phosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetylglucosamine 6-phosphate
N-acetylglucosamine-6-phosphate
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allosteric activator of NagB
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
D-fructose 6-phosphate
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pH 7.7, 30°C, in presence of 0.5 mM N-acetylglucosamine 6-phosphate
0.26 - 9
D-glucosamine 6-phosphate
31.4 - 35.4
NH4+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
107 - 158
alpha-D-glucosamine 6-phosphate
455
D-fructose 6-phosphate
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pH 7.7, 30°C
0.044 - 1800
D-glucosamine 6-phosphate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.4
2,5-anhydro mannitol 6-phosphate
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pH 7.7, 30°C
0.002 - 0.0043
2-deoxy-2-amino-D-glucitol 6-phosphate
1.3
D-fructose oxime 6-phosphate
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pH 7.7, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
pH 6.0: about 25% of maximal activity, pH 8.5: about 60% of maximal activity
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
effect of temperature on homotropic co-operativity in the enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29700
185000
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gel filtration
190000
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pore-gradient gel electrophoresis, density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 28000-30000, SDS-PAGE
hexamer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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enzyme is chemically transaminated, modifying its N-terminal methionine residue to a 2-oxo-4-(methylthio)butyryl group, the transamination markedly reduces the affinity of the enzyme for its allosteric activator N-acetylglucosamine 6-phosphate, in contrast with the unmodified enzyme, which behaves as a typical allosteric K-enzyme, the modified enzyme becomes a mixed K-V allosteric protein, borohydride reduction to obtain the corresponding enzyme with a terminal hydroxy group, this enzyme shows significant recovery of the catalytic catalytic activity and its allosteric activation pattern, becomes similar to that found for the unmodified enzyme; the modification by diethyl dicarbonate results in complete inactivation of enzyme
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
structure of the enzyme in complexes with its allosteric activator and with a competitive inhibitor
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the crystallographic structure of F174A is determinated
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the structure of five complexes of the enzyme in R and T state is described and their kinetic and allosteric implication analysed, the ligand-free enzyme, T-conformer, undergoes an allosteric transition to the free active-site R conformer upon binding of the allosteric activator
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C118Ser/C228S/C239S/D165C/S206W
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the mutant shows reduced turnover number compared to the wild type enzyme
C118S/C228S/C239S
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decrease in kcat-value, no modification of allosteric activation
C219S
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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
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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
D141N
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the mutation modifies the kcat versus pH profile of the enzyme
D141N/E148Q
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mutation modifies the kcat versus pH profile of the enzyme
E148Q
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the mutation modifies the kcat versus pH profile of the enzyme
F174A
H143Q
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drastically impairs the activity of the enzyme in the forward but not in the backward direction of the reaction
K208E
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entirely inactive in absence of allosteric activator N-acetylglucose-6-phosphate
K208V
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homotropic cooperativity, Hill-coefficient 1.7, 2fold increase in dissociation constant for allosteric activator N-acetylglucose-6-phosphate compared to wild-type
R172A
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inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant
R172A/K208E
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inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant
W15Y
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mutant containing a single Trp residue at W224
W15Y/F174W/W224Y
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mutant containing a single, new Trp-residue at F174W
W15Y/W224Y
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mutant without Trp residues
W15Y/W224Y/Y254W
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mutant containing a single, new Trp-residue at Y254W
W224Y
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mutant containing a single Trp residue at W15
Y121T
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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
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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
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the mutant is less active than wild-type enzyme, the replacement causes an uncoupling of the homotropic and heterotrophic effects
Y254T
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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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile to freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, little loss of activity after 2-3 months
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-20°C, in 150 mM Tris-HCl buffer, pH 7.25, 50% v/v glycerol, stable up to 6 months
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0-5°C, in liquid N2, little loss of activity after 2-5 months
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
N-6-aminohexanoyl-glucosamine 6-phosphate agarose column chromatography
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wild-type enzyme and two mutants
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain LAA20
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Comb, D.G.; Roseman, S.
Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase
J. Biol. Chem.
232
807-827
1958
Escherichia coli, Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Midelfort, C.F.; Rose, I.A.
Studies on the mechanism of Escherichia coli glucosamine-6-phosphate isomerase
Biochemistry
16
1590-1596
1977
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Escherichia coli (P0A759)
Manually annotated by BRENDA team
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