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S466E
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mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme in vitro
S466E/S483E
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the double mutant is not phosphorylated by protein kinase B, mutation decreases Km of beta-D-fructose 6-phosphate in vitro
S483E
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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
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site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C238F
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site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C295A
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site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
C295F
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site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
E190Q
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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
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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
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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
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mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
R359A
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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
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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
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the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values
A44V
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the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values
K172A
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increase in Km of beta-D-fructose 6-phosphate
K172E
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increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
K172H
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increase in Km of MgATP2-
K172R
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increase in Km of beta-D-fructose 6-phosphate
K51A
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increase in Km of beta-D-fructose 6-phosphate
K51H
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increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
L148N
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inactive mutant enzyme
L168A
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inactive mutant enzyme
L168R
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mutant enzyme shows 0.2% of wild-type activity
P2R
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kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R136K
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increase in Km of MgATP2-
R136L
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increase in Km of beta-D-fructose 6-phosphate
R193H
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increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
R193L
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increase in Km of beta-D-fructose 6-phosphate
R78H
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increase in Km of MgATP2-
R78L
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increase in Km of MgATP2-
R79H
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increase in Km of MgATP2-
R79L
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increase in Km of MgATP2-
S32A/H258A
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site-directed mutagenesis, increased activity and incresaed expression level in recombinant HEK-293 cells compared to the wild-type enzyme
S32A/H258A
mutant unable to be phosphorylated
additional information
the deletion of N-terminal 318 amino acids abolishes the Michaelis-Menten kinetics of enzyme, Km of beta-D-fructose 6-phosphate is increased, whereas Km of ATP is not significantly altered. When the first 66 amino acids are deleted, the activity ration between 6-phosphofructo-2-kinase and beta-D-fructose 2,6-bisphosphatase is halved. The deletion of 125, 179, 249 and 318 amino acids results in progressive further decreases in the activity ratio and the activity ratio is reduced 4fold when N-terminus is deleted completely. The full-length enzyme is eluted as a tetramer, whereas the truncated enzymes are eluted as monomers
additional information
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mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
additional information
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the chicken enzyme in which the C-termini tail were replaced with that of rat enzyme is not activated by ATP
additional information
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a series of C-terminal deletion mutants are generated: 15, 20, 25 and 30 amino acids, the deletion of the C-terminal 25 or 30 residues of enzyme increases Km of beta-D-fructose 6-phosphate by approximately 2fold. The mutations E446A, H444A, H444K, H444E, R445E, R445L prove the importance of His444 and Arg445.The C-terminal region I involves in the activation of enzyme by ATP.
additional information
construction of a chimeric mutant fusing the N-terminal portion of residues 1-444 of the human enzyme to the C-terminal part, residues 450-530, of the Bos taurus enzyme, i.e. HBPBHP, construction of a deletion mutant lacking the entire carboxyterminal region of residues 446-519
additional information
knockdown of PFKFB4 in prostate cancer cells by specific shRNA targeting
additional information
siRNA silencing of endogenous PFKFB3 in HeLa cells by siRNA
additional information
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siRNA silencing of endogenous PFKFB3 in HeLa cells by siRNA
additional information
stable shRNA knockdown of PFKFB4, silencing by siRNA and genomic deletion of PFKFB4 decrease fructose 2,6-bisphosphate. PFKFB4 overexpression increases fructose 2,6-bisphosphate and selective PFKFB4 inhibition in vivo markedly reduces fructose 2,6-bisphosphate, glucose uptake, and ATP levels
additional information
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additional information
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effects of N- and C-terminal deletions of skeletal muscle and liver enzyme, e.g. ND4, ND7, ND12, ND23, CD30, comparison of the kinetic properties of deletion mutants
additional information
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mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
additional information
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ATP binding and the effect of pH on the kinetics are characterized
additional information
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mutant enzyme, in which the four tryptophan residues in the isoenzyme are mutated to phenylalanine, structure
additional information
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enzyme contains four tryptophan residues: Trp15, Trp64, Trp299 and Trp320, mutant enzymes contain either no Trp or a single Trp at each location, the other Trp residues having been converted to Phe, mutations do not cause large change in protein conformation and function, Trp299 and Trp320 in mutant enzymes quenched by iodide to a small extent can indicate an altered conformation, Trp64 is not accessible
additional information
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engineering of the LKVWT glucokinase-binding motif in the FBPase-2 domain of islet PFK-2/FBPase-2 to HKEWR leads to significantly lower interaction with glucokinase compared with wild-type at 25 mmol/liter glucose
additional information
generation of a fluorescent PFK2/FBPase2-YC155 construct
additional information
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generation of a fluorescent PFK2/FBPase2-YC155 construct
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