Information on EC 2.7.1.4 - fructokinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.1.4
-
RECOMMENDED NAME
GeneOntology No.
fructokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-fructose = ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
D-sorbitol degradation I
-
-
Fructose and mannose metabolism
-
-
heterolactic fermentation
-
-
mannitol cycle
-
-
Metabolic pathways
-
-
metabolism of disaccharids
-
-
Starch and sucrose metabolism
-
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sucrose degradation I (sucrose phosphotransferase)
-
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sucrose degradation II (sucrose synthase)
-
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sucrose degradation III (sucrose invertase)
-
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sucrose degradation IV (sucrose phosphorylase)
-
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sucrose degradation VII (sucrose 3-dehydrogenase)
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-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose 6-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-51-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
sugar beet
SwissProt
Manually annotated by BRENDA team
induction by D-fructose, repression by D-glucose, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
camellia
-
-
Manually annotated by BRENDA team
pepper
-
-
Manually annotated by BRENDA team
expression in Corynebacterium glutamicum
-
-
Manually annotated by BRENDA team
strain ZJU 8235
-
-
Manually annotated by BRENDA team
strain ZJU 8235
-
-
Manually annotated by BRENDA team
K-12
-
-
Manually annotated by BRENDA team
honey locust
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
B8GZ52
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain WCFS1
-
-
Manually annotated by BRENDA team
fructokinase I: induced specifically by growth on sucrose
-
-
Manually annotated by BRENDA team
strain ATCC12291
TrEMBL
Manually annotated by BRENDA team
strain ATCC12291
TrEMBL
Manually annotated by BRENDA team
lily
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
cultivar Samsun
-
-
Manually annotated by BRENDA team
avocado
-
-
Manually annotated by BRENDA team
hybrid aspen wood: Populus tremula- Populus tremuloides
-
-
Manually annotated by BRENDA team
KN-21
-
-
Manually annotated by BRENDA team
KN-21
-
-
Manually annotated by BRENDA team
bv.trifolii
-
-
Manually annotated by BRENDA team
var N19, isoforms FRK1 and FRK2
-
-
Manually annotated by BRENDA team
male worms
-
-
Manually annotated by BRENDA team
Mill.
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
expression in Escherichia coli with C-terminal His-tag
-
-
Manually annotated by BRENDA team
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A5EZZ9
UniProt
Manually annotated by BRENDA team
-
A5EZZ9
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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RNAi-mediated reduction of FRK2 activity in developing wood of hybrid aspen lead to the accumulation of soluble neutral sugars and a decrease in hexose phosphates and UDP-glucose. Reduced FRK2 activity also leads to thinner fiber cell walls with a reduction in the proportion of cellulose
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
CTP + D-fructose
CDP + D-fructose 6-phosphate
show the reaction diagram
D-fructose + ATP
D-fructose 6-phosphate + ADP
show the reaction diagram
dATP + D-fructose
dADP + D-fructose 6-phosphate
show the reaction diagram
GTP + D-fructose
GDP + D-fructose 6-phosphate
show the reaction diagram
ITP + D-fructose
IDP + D-fructose 6-phosphate
show the reaction diagram
TTP + D-fructose
TDP + D-fructose 6-phosphate
show the reaction diagram
UTP + D-fructose
UDP + D-fructose 6-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
additional information
?
-
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discussion of possible significance of the enzyme in plant carbohydrate metabolism
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
-
inhibitory at low and stimulatory at high ATP concentration
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
can partially replace Mg2+ in activation
Sr2+
-
1% of activity with Mg2+
Zn2+
-
can partially replace Mg2+ in activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta,gamma-methyleneadenosine 5'-triphosphate
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-
Ca2+
-
slightly inhibitory at 0.1 mM
CTP
-
above 1 mM
D-fructose
D-fructose 6-phosphate
D-galactose
-
30% inhibition at 10 mM
D-glucosamine
-
65% inhibition at 10 mM
D-glucose
D-glucose 6-phosphate
D-mannose
-
59% inhibition at 10 mM
GTP
-
above 1 mM
L-sorbose
-
-
MgADP-
MgATP2-
Mn2+
-
can partially replace Mg2+ in activation, inhibition above 0.5 mM at 1 mM ATP
additional information
not inhibitory: D-glucose, and Mg2+ up to 10 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024 - 1.3
ATP
0.156 - 0.268
CTP
0.006 - 3.3
D-fructose
0.14
D-glucose
-
30C, pH 8
0.9
D-GTP
-
FKII, pH 8, 25C
0.4
D-mannose
-
pH 6.9, 25C
0.1 - 0.7
fructose
0.132 - 0.69
GTP
0.25
ITP
-
; pH 7.4, 30C
0.06 - 0.2
MgATP2-
0.15 - 1.86
UTP
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
494 - 8897
D-fructose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 2.5
ADP
0.0161 - 21
D-fructose
1.3
D-fructose 6-phosphate
-
FK 1, pH 8
0.16 - 0.2
MgATP2-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00746
-
at 25C
0.094
-
-
0.84
-
substrate D-fructose, pH 6.5, 50C
1.8
-
substrate ATP, pH 6.5, 50C
11.2
-
-
18.83
-
isoform FRK1, pH 8.0, 25C
44.05
-
isoform FRK1, pH 8.0, 25C
51.8
-
fructokinase Ia and Ib
60.3
-
fructokinase II
240
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S69A mutant
250
-
wild-type
730
-
substrate D-fructose, pH 7.5, 80C
835
pH 8.5, 30C
920
-
substrate ATP, pH 7.5, 80C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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7 - 8.5
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D-fructose
7.5 - 8.5
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-
7.5 - 9.5
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broad with maximum at pH 8.5
7.8 - 8.5
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-
8.8 - 10
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lengthy plateau in the alkaline zone
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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marked decrease in activity below and above
6 - 8.5
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pH 6: about 55% of activity maximum, pH 8.5: about 35% of activity maximum
6
-
30% loss of activity, both isoform FRK1 and FRK2
6.7 - 9.3
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pH 6.7: about 50% of activity maximum, pH 9.3: about 60% of activity maximum
7.4 - 9.3
-
more than 90% of activity maximum at pH 7.4 and pH 9.3
7.4 - 8.4
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more than 90% of activity maximum at pH 7.4 and pH 8.4
7.5 - 9
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both isoform FRK1 and FRK2
10
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40% loss of activity, both isoform FRK1 and FRK2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
11.7% of activity at 80C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.65
-
IsoGel agarose
4.8
-
three polypeptides, one-dimensional isoelectric focusing
4.87
calculated
5.34
calculated
5.6 - 5.9
-
polypeptide 1, pre-cast Ampholine PAGplates at 10C
5.66 - 6.17
-
six closely grouped peptides, two-dimensional isoelectric focusing/SDS-PAGE
6.07 - 6.55
-
4 components, FKII, two-dimensional isoelectric focusing/SDS-PAGE
6.42 - 6.55
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2 components, FKI, two-dimensional isoelectric focusing /SDS-PAGE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
expressed in all organs examined
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562)
Rhizobium meliloti (strain 1021)
Ruegeria sp. (strain TM1040)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000 - 80000
-
glycerol gradient equilibrium sedimentation in the presence of MgATP2-
20000
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glycerol gradient equilibrium sedimentation in presence of 10 mM fructose or 10 mM MgCl2
34000
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SDS-PAGE
36500
-
SDS-PAGE
37000
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fructokinase-Ia, and fructokinase-1b, gel filtration
39000
-
SDS-PAGE
44000
-
gel filtration
47000
-
sucrose density gradient centrifugation
58000
-
gel filtration
59000
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gel filtration
60000
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nondenaturing equilibrium ultracentrifugation
69000
-
gel filtration, both isoform FRK1 and FRK2
72000
-
gel filtration
72400
-
gel filtration
75000
-
gel filtration
80000
-
glycerol gradient equilibrium sedimentation in presence of 10 mM MgATP2-
84000
-
gel filtration
85000
-
native enzyme
102000
-
FK 1, gel filtration
105000
-
FK 1, gel filtration
118000
-
FK 1, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structures of ROK FK from Bacillus subtilis (a) apo and in the presence of (b) ADP and (c) ADP/D-fructose is shown. All structures show that YdhR is a homo-dimer with a monomer composed of two similar alpha/beta domains forming a large cleft between domains that bind ADP and D-fructose
crystal structure of a FRK homolog from Halothermothrix orenii refined to 2.8 A resolution is reported. The structure of the Hore_18220 protein reveals a catalytic domain with a Rossmann-like fold and a beta-sheet lid for dimerization
B8GZ52
Crystals of Vibrio cholerae Vc-FK and its cocrystal with fructose, ADP and Mg2+ are grown in the presence of polyethylene glycol 6000 and diffracted to 2.45 and 1.75 A resolution, respectively
A5EZZ9
hanging drop vapor diffusion method
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
1 h, 50% loss of activity
641497
6.5 - 8
-
maximal stability
641477
6.5 - 8.5
-
stable
641507
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 40
-
gradual decrease of activtiy in this range
37 - 39
-
15 min, 70% residual activity
40
after 1 h the residual activity is 80%
50
after 5 min the residual activity is 20%
80
-
4 h, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT, 10 mM, necessary to stabilize activity
-
freezing and thawing after elution from the first DEAE-cellulose column results in 30% loss of activity
-
increased heat lability in presence of fructose
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metal binding agents protect
-
no significant loss of activity after lyophilization and reconstitution of the enzyme
-
stable after repeated freezing, at -20C, and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, stable for at least 2 months
-
-20C, in presence of Mg2+ and dithiothreitol, 25% loss of activity after 6 months
-
-80C, PBS buffer, stable for at least 3 months
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0C, 0.2 (NH4)2SO4, pH 7.0, stable for several months
-
2C, pH 7, in presence of Mg2+ and dithioerythritol, 25% loss of activity after 2 weeks
-
4C, 0.2 mM imidazole buffer (pH 8.0), two months
4C, 50% loss of activity after 24 h
-
5C, stable for 6 weeks at pH 8
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-step purification leads to highly purified enzyme
-
3 forms: FK-I, FK-II and FK-III
-
400fold, FKI and FKII
-
FK1, FK2, FK3
-
homogeneity
-
isoenzyme FK-I, FK-II
-
isoenzyme fructokinase III
-
isoforms FRK1 and FRK2
-
partial
partial, 3 forms: fructokinase-Ia,-Ib,-II
-
purification of UTP-dependent enzyme: CTP, GTP and UTP are more effective as phosphate donors than ATP, organism also has a nonspecific fructokinase and a third fairly specific activity for ATP
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purified using Ni-NTA affinity chromatography
A5EZZ9
recombinant protein
-
Sephadex G25 column chromatography; Sephadex G25 column chromatography
using metal chelate affinity chromatography
using Ni-NTA chromatography
using Ni-NTA-chromatography and gel filtration
B8GZ52
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli strain XL1-Blue
expression of Zymomonas mobilis gene in Escherichia coli
-
overexpressed in Escherichia coli BL21 as a His-taggeg fusion protein
A5EZZ9
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
hepatic KHK and AldoB expression are increased 2.7fold and 1.8fold, respectively, in fructose-fed rats compared to control rats
-
uric acid up-regulates KHK expression thus leading to the amplification of the lipogenic effects of fructose
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S69A
-
more thermostable than wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
enzyme expression strategy for enhancing amino acid production
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