BRENDA - Enzyme Database
show all sequences of 2.7.1.B27

Synthesis and physicochemical characterization of D-tagatose-1-phosphate: the substrate of the tagatose-1-phosphate kinase in the phosphotransferase system-mediated D-tagatose catabolic pathway of c

Van der Heiden, E.; Delmarcelle, M.; Simon, P.; Counson, M.; Galleni, M.; Freedberg, D.I.; Thompson, J.; Joris, B.; Battistel, M.D.; J. Mol. Microbiol. Biotechnol. 25, 106-119 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene tagK, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
Bacillus licheniformis
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-fructose-6-phosphate
-
Bacillus licheniformis
D-tagatose 6-phosphate
-
Bacillus licheniformis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics, the catalytic efficiency of the enzyme for D-tagatose 1-phosphate of 137.5 M/s is 40fold higher than that for fructose 1-phosphate with 3.4 M/s, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
Bacillus licheniformis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Bacillus licheniformis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + D-tagatose 1-phosphate
Bacillus licheniformis
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
ATP + D-tagatose 1-phosphate
Klebsiella oxytoca
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
ATP + D-tagatose 1-phosphate
Klebsiella oxytoca M5a1
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
ATP + D-tagatose 1-phosphate
Bacillus licheniformis ATCC 14580
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus licheniformis
Q65EY9
annotated as fructose-1-phosphate kinase; gene tagK or BL01904
-
Bacillus licheniformis ATCC 14580
Q65EY9
annotated as fructose-1-phosphate kinase; gene tagK or BL01904
-
Klebsiella oxytoca
Q8VS15
annotated as 1-phosphofructokinase; gene tagK
-
Klebsiella oxytoca M5a1
Q8VS15
annotated as 1-phosphofructokinase; gene tagK
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) b nickel affinity chromatography and desalting gel filtration
Bacillus licheniformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + D-tagatose 1-phosphate
-
738891
Bacillus licheniformis
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
-
738891
Klebsiella oxytoca
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
the enzyme is absolutely substrate-specific, determination of the phosphate positions by NMR spectroscopy
738891
Bacillus licheniformis
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
-
738891
Klebsiella oxytoca M5a1
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
-
738891
Bacillus licheniformis ATCC 14580
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
the enzyme is absolutely substrate-specific, determination of the phosphate positions by NMR spectroscopy
738891
Bacillus licheniformis ATCC 14580
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate
738891
Klebsiella oxytoca
?
-
-
-
-
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate. The catalytic efficiency of the enzyme for D-tagatose 1-phosphate is 40fold higher than that for fructose 1-phosphate, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
738891
Bacillus licheniformis
?
-
-
-
-
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate
738891
Klebsiella oxytoca M5a1
?
-
-
-
-
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate. The catalytic efficiency of the enzyme for D-tagatose 1-phosphate is 40fold higher than that for fructose 1-phosphate, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
738891
Bacillus licheniformis ATCC 14580
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Bacillus licheniformis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bacillus licheniformis
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Bacillus licheniformis
ATP
-
Klebsiella oxytoca
Cloned(Commentary) (protein specific)
Commentary
Organism
gene tagK, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
Bacillus licheniformis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Bacillus licheniformis
ATP
-
Klebsiella oxytoca
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-fructose-6-phosphate
-
Bacillus licheniformis
D-tagatose 6-phosphate
-
Bacillus licheniformis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics, the catalytic efficiency of the enzyme for D-tagatose 1-phosphate of 137.5 M/s is 40fold higher than that for fructose 1-phosphate with 3.4 M/s, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
Bacillus licheniformis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Bacillus licheniformis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + D-tagatose 1-phosphate
Bacillus licheniformis
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
ATP + D-tagatose 1-phosphate
Klebsiella oxytoca
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
ATP + D-tagatose 1-phosphate
Klebsiella oxytoca M5a1
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
ATP + D-tagatose 1-phosphate
Bacillus licheniformis ATCC 14580
-
ADP + D-tagatose 1,6-bisphosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) b nickel affinity chromatography and desalting gel filtration
Bacillus licheniformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + D-tagatose 1-phosphate
-
738891
Bacillus licheniformis
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
-
738891
Klebsiella oxytoca
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
the enzyme is absolutely substrate-specific, determination of the phosphate positions by NMR spectroscopy
738891
Bacillus licheniformis
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
-
738891
Klebsiella oxytoca M5a1
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
-
738891
Bacillus licheniformis ATCC 14580
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 1-phosphate
the enzyme is absolutely substrate-specific, determination of the phosphate positions by NMR spectroscopy
738891
Bacillus licheniformis ATCC 14580
ADP + D-tagatose 1,6-bisphosphate
-
-
-
?
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate
738891
Klebsiella oxytoca
?
-
-
-
-
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate. The catalytic efficiency of the enzyme for D-tagatose 1-phosphate is 40fold higher than that for fructose 1-phosphate, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
738891
Bacillus licheniformis
?
-
-
-
-
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate
738891
Klebsiella oxytoca M5a1
?
-
-
-
-
additional information
the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate. The catalytic efficiency of the enzyme for D-tagatose 1-phosphate is 40fold higher than that for fructose 1-phosphate, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
738891
Bacillus licheniformis ATCC 14580
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Bacillus licheniformis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bacillus licheniformis
General Information
General Information
Commentary
Organism
additional information
structure homology modeling of tagatose-1P kinase using the structure of fructose 1-phosphate kinase from Bacillus halodurans, PDB ID 2ABQ
Bacillus licheniformis
General Information (protein specific)
General Information
Commentary
Organism
additional information
structure homology modeling of tagatose-1P kinase using the structure of fructose 1-phosphate kinase from Bacillus halodurans, PDB ID 2ABQ
Bacillus licheniformis
Other publictions for EC 2.7.1.B27
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738891
Van der Heiden
Synthesis and physicochemical ...
Bacillus licheniformis, Bacillus licheniformis ATCC 14580, Klebsiella oxytoca, Klebsiella oxytoca M5a1
J. Mol. Microbiol. Biotechnol.
25
106-119
2015
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