BRENDA - Enzyme Database
show all sequences of 2.7.1.56

Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase

Pickl, A.; Johnsen, U.; Schoenheit, P.; J. Bacteriol. 194, 3088-3097 (2012)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.08
-
ATP
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
0.31
-
D-Fructose 1-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
1.12
-
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
the enzyme shows the highest activity at about 0.5M KCl
Haloferax volcanii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38000
-
2 * 38000, SDS-PAGE
Haloferax volcanii
70000
-
gel filtration
Haloferax volcanii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + D-fructose 1-phosphate
Haloferax volcanii
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
?
ATP + D-fructose 1-phosphate
Haloferax volcanii H1209
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
?
ATP + D-fructose 6-phosphate
Haloferax volcanii
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + ?
-
-
?
ATP + D-fructose 6-phosphate
Haloferax volcanii H1209
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + ?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haloferax volcanii
D4GYE6
-
-
Haloferax volcanii H1209
D4GYE6
-
-
Purification (Commentary)
Commentary
Organism
Ni-NTA column chromatography and Superdex 200 gel filtration
Haloferax volcanii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + D-fructose 1-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 1-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii H1209
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii
ADP + ?
-
-
-
?
ATP + D-fructose 6-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii H1209
ADP + ?
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 38000, SDS-PAGE
Haloferax volcanii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
9
-
Haloferax volcanii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.08
-
ATP
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
0.31
-
D-Fructose 1-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
1.12
-
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
the enzyme shows the highest activity at about 0.5M KCl
Haloferax volcanii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38000
-
2 * 38000, SDS-PAGE
Haloferax volcanii
70000
-
gel filtration
Haloferax volcanii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + D-fructose 1-phosphate
Haloferax volcanii
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
?
ATP + D-fructose 1-phosphate
Haloferax volcanii H1209
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
?
ATP + D-fructose 6-phosphate
Haloferax volcanii
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + ?
-
-
?
ATP + D-fructose 6-phosphate
Haloferax volcanii H1209
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
ADP + ?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
Ni-NTA column chromatography and Superdex 200 gel filtration
Haloferax volcanii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + D-fructose 1-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 1-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii H1209
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii
ADP + ?
-
-
-
?
ATP + D-fructose 6-phosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
722543
Haloferax volcanii H1209
ADP + ?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 38000, SDS-PAGE
Haloferax volcanii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
9
-
Haloferax volcanii
Expression
Organism
Commentary
Expression
Haloferax volcanii
enzyme expression is specifically upregulated in fructose-grown cells
up
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in fructose catabolism
Haloferax volcanii
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in fructose catabolism
Haloferax volcanii
Expression (protein specific)
Organism
Commentary
Expression
Haloferax volcanii
enzyme expression is specifically upregulated in fructose-grown cells
up
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
34
-
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
1200
-
D-Fructose 1-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
34
-
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
1200
-
D-Fructose 1-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
Haloferax volcanii
Other publictions for EC 2.7.1.56
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)
738617
Chan
Yeast phosphofructokinase-1 su ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
J. Biol. Chem.
289
19448-19457
2014
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23
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-
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1
1
-
-
-
737595
Funato
Nucleoredoxin regulates glucos ...
Mus musculus
Biochem. Biophys. Res. Commun.
440
737-742
2013
-
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-
-
-
-
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1
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4
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4
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1
1
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722543
Pickl
Fructose degradation in the ha ...
Haloferax volcanii, Haloferax volcanii H1209
J. Bacteriol.
194
3088-3097
2012
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3
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1
2
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5
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1
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1
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1
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4
1
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1
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1
1
1
1
2
2
684377
Su
Human H+ATPase a4 subunit muta ...
Homo sapiens
Am. J. Physiol. Renal Physiol.
295
F950-F958
2008
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1
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1
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1
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1
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687484
Peskov
Kinetic model of phosphofructo ...
Escherichia coli
J. Bioinform. Comput. Biol.
6
843-867
2008
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1
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687740
Deng
Phosphorylation of Bad at Thr- ...
Mus musculus
J. Biol. Chem.
283
20754-20760
2008
-
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1
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1
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1
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1
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1
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1
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688049
Russell
Some characteristics of rabbit ...
Oryctolagus cuniculus
J. Enzyme Inhib. Med. Chem.
23
411-417
2008
-
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-
-
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-
1
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1
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1
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686728
Martinez-Costa
Chimeric phosphofructokinases ...
Homo sapiens
FEBS Lett.
581
3033-3038
2007
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-
1
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1
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1
1
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1
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1
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2
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661250
Hagopian
Fructose metabolizing enzymes ...
Mus musculus
Biochim. Biophys. Acta
1721
37-43
2005
-
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1
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3
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1
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2
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674240
Barriere
Fructose utilization in Lactoc ...
Lactococcus lactis, Lactococcus lactis JIM8240
J. Bacteriol.
187
3752-3761
2005
-
-
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5
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2
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1
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2
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641686
Veiga-da-Cunha
Overexpression and purificatio ...
Escherichia coli
Protein Expr. Purif.
19
48-52
2000
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-
1
-
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4
-
1
1
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-
2
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1
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1
1
1
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1
1
1
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727057
Rangaswamy
Characterization of 1-phosphof ...
Haloarcula vallismortis, Haloarcula vallismortis ATCC 34679
Biochim. Biophys. Acta
1201
106-112
1994
1
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6
2
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6
1
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5
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1
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10
1
1
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1
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1
1
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6
1
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1
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10
1
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1
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1
1
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641683
Buschmeier
-
Purification and properties of ...
Escherichia coli
FEMS Microbiol. Lett.
29
231-235
1985
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4
2
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2
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1
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2
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2
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1
1
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2
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641685
Bang
Properties of 1-phosphofructok ...
Pseudomonas putida
Can. J. Microbiol.
23
721-725
1977
1
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4
3
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5
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1
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3
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1
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1
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1
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1
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1
1
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640495
Baumann
Catabolism of D-fructose and D ...
Oceanimonas doudoroffii
Arch. Microbiol.
105
241-248
1975
-
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6
2
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5
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2
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1
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3
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1
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6
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1
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3
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1
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1
1
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641680
Anderson
D-fructose-1-phosphate kinase ...
Klebsiella aerogenes
Methods Enzymol.
42C
63-66
1975
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1
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2
1
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1
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1
4
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1
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641681
Van Hugo
Purification and properties of ...
Clostridium pasteurianum
Eur. J. Biochem.
48
455-463
1974
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2
12
3
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7
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2
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1
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12
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5
7
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1
2
1
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1
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641682
Du Toit
-
Properties of 1-phosphofructok ...
Clostridium pasteurianum
Enzymologia
43
285-300
1972
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1
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1
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640483
Sapico
D-fructose 1-phosphate kinase ...
Klebsiella aerogenes
J. Biol. Chem.
244
6280-6288
1969
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7
2
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1
1
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8
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7
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1
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1
2
8
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1
1
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641677
Hanson
D-fructose 1-phosphate kinase, ...
Klebsiella aerogenes
J. Biol. Chem.
241
1644-1645
1966
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2
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641679
Reeves
1-Phosphofructokinase from an ...
Clostridium symbiosum
J. Biol. Chem.
241
1257-1261
1966
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2
1
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6
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6
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