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2.7.1.11: 6-phosphofructokinase

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

Word Map on EC 2.7.1.11

Reaction

ATP
+
beta-D-fructofuranose 6-phosphate
=
ADP
 +
beta-D-fructofuranose 1,6-bisphosphate

Synonyms

1-phosphofructokinase, 2-keto-3-deoxygluconate kinase, 6-phosphofructo 1-kinase, 6-phosphofructo-1-kinase, 6-phosphofructokinase I, 6-phosphofructokinase, platelet type, 6-phosphofructose 1-kinase, 6-phosphofructose-1-kinase, A/GTP-PFK, ADP-dependent phosphofructokinase, APE0012, At2g22480, At4g26270, At4g29220, At4g32840, At5g56630, At5g61580, ATP-dependent 6-phosphofructokinase, ATP-dependent 6-phosphofructokinase isozyme 2, ATP-dependent PFK, ATP-dependent phosphofructokinase, ATP-PFK, ATP: D-fructose-6-phosphate-1-phosphotransferase, ATP:D-fructose-6-phosphate-1-phosphotransferase, D-fructose-6-phosphate 1-phosphotransferase, fructose 6-phosphate kinase, fructose 6-phosphokinase, hosphofructokinase-1, HVO_A0328, KDG kinase, KDGal kinase, KDGK-1, KDGK-2, kinase, phosphofructo- (phosphorylating), LmPFK, muscle-type phosphofructokinase, nucleotide triphosphate-dependent phosphofructokinase, OC_Os04g39420, PFK, PFK-1, Pfk-2, PFK-L, PFK-M, PFK-P, PFK1, PFK2, PFK3, PFK4, PFK5, PFK6, PFK7, PFKA, PFKA1, PFKA2, PFKA3, pfkB, PFKL, PFKM, PFKMS, PFKP, PfpA4, phospho-1,6-fructokinase, phosphofructo-1-kinase, phosphofructokinase, phosphofructokinase 1, phosphofructokinase M, phosphofructokinase-1, phosphofructokinase-2, phosphofructokinase-M, phosphofructokinase-P, phosphohexokinase, TbPFK, TcPFK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.11 6-phosphofructokinase

Engineering

Engineering on EC 2.7.1.11 - 6-phosphofructokinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D127/R252Q
-
very low activity, unchanged Km for fructose 6-phosphate
D127S
-
almost no activity
E190Q
-
the mutation drastically diminishes the kinetic affinity of this site for Mg2+ and Mn2+
E222A/H223A
-
ability to be allosterically regulated is retained
F76A
62fold increase in Km for ATP
F76W
apparant Kms for ATP, ITP, GTP, CTP and UTP
F76Y
apparant Kms for ATP, ITP, GTP, CTP and UTP
H249E
-
ability to be allosterically regulated is retained, inhibition by phosphoenol pyruvate is lost
I126A
-
600fold lower affinity for fructose 6-phosphate than wild-type, modestly lower Kcat than wild-type, greater ATP inhibition at pH 6.0 and 7.0 than at pH 8.0
L93A
single-point mutant, constructed to destabilize the interface of isoform Pfk2. The mutant is an inactive monomer at protein concentrations below 30 microM. Active dimer formation can be induced by increasing the protein concentration and by addition of its substrate fructose-6-phosphate. Unfolding occurs noncooperatively and the isolated subunit is partially unstructured and marginally stable
M169A
M169L
6fold lower kcat than wild-type
R111E
apparant Kms for ATP, ITP, GTP, CTP and UTP
R11A
apparant Kms for ATP, ITP, GTP, CTP and UTP
R162E
-
ability to be allosterically regulated is retained
R171E
-
approx. 6% of wild-type catalytic activity
R243E
-
ability to be allosterically regulated is retained
R252E
-
allosteric response to MgATP2- is lost, inhibition by phosphoenol pyruvate is lost
R252Q
-
50fold decrease in Kcat, 1600fold increase in Km for fructose 6-phosphate
R25S
not activated by GDP, pattern of ATP inhibition nearly identical to wild-type
R72E
-
approx. 0.5% of wild-type catalytic activity
R72H
-
almost no PFK activity
R77A
apparant Kms for ATP, ITP, GTP, CTP and UTP
R77D
apparant Kms for ATP, ITP, GTP, CTP and UTP
R77E
apparant Kms for ATP, ITP, GTP, CTP and UTP
R77L
apparant Kms for ATP, ITP, GTP, CTP and UTP
R82A
20fold increase in Km for ATP
R82E
apparant Kms for ATP, ITP, GTP, CTP and UTP
T125A
-
almost no activity detectable
Y41A
49fold increase in Km for ATP
Y41F
apparant Kms for ATP, ITP, GTP, CTP and UTP
Y41L
apparant Kms for ATP, ITP, GTP, CTP and UTP
Y41W
apparant Kms for ATP, ITP, GTP, CTP and UTP
I126A
-
600fold lower affinity for fructose 6-phosphate than wild-type, modestly lower Kcat than wild-type, greater ATP inhibition at pH 6.0 and 7.0 than at pH 8.0
-
R72H
-
almost no PFK activity
-
G212V
I150V
Km-value for D-fructose 6-phosphate is 1.1fold lower than the wild-type value
I153V
mutation has a substantial positive impact on the magnitude of inhibition by phosphoenolpyruvate
I234V
Km-value for D-fructose 6-phosphate is comparable to the wild-type value
K90/91E
-
surface charge-tag substitution, no change in Km for ATP and K1/2 for fructose 6-phosphate
R162E
-
single active site substitution, affinity for fructose 6-phosphate is diminished approx. 3 orders of magnitude relative to that of the wild-type
R211E/K213E
-
allosteric site substitutions
D543A
-
the mutation causes an increased efficacy of ATP at the inhibitory allosteric binding site. The mutation drastically increases K0.5 for AMP. The activating effect of ADP found in wild type enzyme is completely lost
D564N
somatic mutation identified in human cancers. Mutant has decreased maximum velocity and affinity for fructose 6-phosphate
E657A
mutant has reduced affinity of about 4.5 mM for frucotse 6-phosphate, compared with about 0.8 mM in wild type, and an 2fold decrease in maximum activity
H242A
-
the mutant enzyme shows reduced Km value for ATP and 38.4% residual activity in the presence of 4.5 mM ADP
K386A
-
the mutant enzyme shows increased Km value for ATP and 33.1% residual activity in the presence of 4.5 mM ADP
K678A
-
the mutant enzyme shows reduced Km value for ATP. Ki values of ADP and ATP remain unchanged
N341A
N341A/R246A/K386A
-
the mutant enzyme shows reduced Km value for ATP and 21.9% residual activity in the presence of 4.5 mM ADP
N426S
somatic mutation identified in human cancers. Mutation partially relieves ATP inhibition
R246A
-
the mutant enzyme shows slightly increased Km value for ATP and 41.7% residual activity in the presence of 4.5 mM ADP
R246A/K386A
-
the mutant enzyme shows increased Km value for ATP and 33.2% residual activity in the presence of 4.5 mM ADP
R48C
somatic mutation identified in human cancers. Residue Arg48 interacts with a bound phosphate ion in the structure, and the mutant shows reduced citrate inhibition
S377A
-
the mutant enzyme shows reduced Km value for ATP. Ki values of ADP and ATP remain unchanged
S377A/K678A
-
the mutant enzyme shows reduced Km value for ATP. Ki values of ADP and ATP are significantly reduced in this mutant
R429A
-
no change in Km for ATP and fructose 6-phosphate, less sensitive to inhibition by ATP
R433A
-
no change in Km for ATP and fructose 6-phosphate, not inhibited by ATP up to 6 mM, Arg433 is probably a component of the inhibitory site for ATP
R481D
-
no alteration in nucleotide binding to inhibitory site, 50% inhibition at 0.4-0.7 mM ATP, 10% of wild-type PFK activation with 0.1 mM fructose 2,6-bisphosphate
R481L
-
no alteration in nucleotide binding to inhibitory site, 50% inhibition at 0.4-0.7 mM ATP
R48L
-
similar specific activity as wild-type, less sensitive to ATP inhibition, not inhibited by citrate and 3-phosphoglycerate
G150D/L151A
L313W
additional information