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2.7.1.105: 6-phosphofructo-2-kinase

This is an abbreviated version!
For detailed information about 6-phosphofructo-2-kinase, go to the full flat file.

Word Map on EC 2.7.1.105

Reaction

ATP
+
beta-D-fructose 6-phosphate
=
ADP
+
beta-D-fructose 2,6-bisphosphate

Synonyms

6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase-2, 6-phosphofructo kinase-2/fructose diphosphatase-2 isoenzyme 3, 6-phosphofructo-2-kinase, 6-phosphofructo-2-kinase/2,6-bisphosphatase 3, 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase:glucokinase complex, 6-phosphofructose 2-kinase, 6PF2K/Fru-2,6-P2ase, ATP:D-fructose-6-phosphate 2-phosphotransferase, fructose 6-phosphate 2-kinase, inducible 6-phosphofructo-2-kinase, iPFK2, kinase, 6-phosphofructo-2-(phosphorylating), OsF2KP1, OsF2KP2, Pfk-2, PFK-2/FBPase, PFK-2/FBPase-2, PFK2, PFK2/FBPase2, PFKFB, PFKFB-3, PFKFB1, PFKFB2, PFKFB3, PFKFB4, phosphofructokinase 2, phosphofructokinase-2, phosphofructokinase-2/fructose bisphosphatase-2, T-PFK2, tPFK-2, uPFK-2

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.105 6-phosphofructo-2-kinase

Engineering

Engineering on EC 2.7.1.105 - 6-phosphofructo-2-kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S466E
-
mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme in vitro
S466E/S483E
-
the double mutant is not phosphorylated by protein kinase B, mutation decreases Km of beta-D-fructose 6-phosphate in vitro
S483E
-
mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme and mutation decreases citrate inhibition in vitro
C238A
-
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C238F
-
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C295A
-
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
C295F
-
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
E190Q
-
mutant presents a 50fold decrease in the kcat value and a 15fold increment in the apparent Km for MgATP2+. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
L307A
-
site-directed mutagenesis, C-terminal point mutant, further mutants analyzed that reveal successive deletions of up to 10 residues at the C-terminal end
Y306A
-
site-directed mutagenesis, C-terminal point mutant, no dimer-tetramer conversion in presence of MgATP, inhibition pattern almost undistinguishable from the wild-type, conformational changes leading to allosteric inhibition can be uncoupled from tetramer formation at least in the Y306A mutant
R279A
-
mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
R359A
-
mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
H253A
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
H253A/S460D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
K472/473A
mutant fails to localize in nucleus, mainly localizes in cytoplasm. The mutant inhibits the autophagic process, stimulates lactate production, and decreases the activity of AMPK compared to the wild-type
K472A/K473A
cytoplasmic mutant
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R75A/R76A
kinase inactive
S302R
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S460D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S460D/T470D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S477D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
T470D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
A44G
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values
A44V
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values
H256A
crystal structure
K172A
-
increase in Km of beta-D-fructose 6-phosphate
K172E
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
K172H
-
increase in Km of MgATP2-
K172R
-
increase in Km of beta-D-fructose 6-phosphate
K51A
-
increase in Km of beta-D-fructose 6-phosphate
K51H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
L148N
-
inactive mutant enzyme
L168A
-
inactive mutant enzyme
L168R
-
mutant enzyme shows 0.2% of wild-type activity
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R136K
-
increase in Km of MgATP2-
R136L
-
increase in Km of beta-D-fructose 6-phosphate
R193H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
R193L
-
increase in Km of beta-D-fructose 6-phosphate
R78H
-
increase in Km of MgATP2-
R78L
-
increase in Km of MgATP2-
R79H
-
increase in Km of MgATP2-
R79L
-
increase in Km of MgATP2-
S32A/H258A
additional information