2.7.1.40: pyruvate kinase
This is an abbreviated version!
For detailed information about pyruvate kinase, go to the full flat file.
Word Map on EC 2.7.1.40
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2.7.1.40
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hexokinase
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phosphofructokinase
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erythrocyte
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fructose
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glucose-6-phosphate
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hepatocytes
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glycogen
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anemia
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carboxykinase
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gluconeogenesis
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aldolase
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pep
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hemolytic
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malate
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citrate
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creatine
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glucokinase
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adenylate
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carboxylase
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warburg
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gluconeogenic
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enolase
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phosphoglycerate
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pentose
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6-phosphate
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malic
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glucagon
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glyceraldehyde-3-phosphate
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reticulocyte
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lipogenesis
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6-phosphogluconate
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fructose-1,6-bisphosphate
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lipogenic
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2,6-bisphosphate
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g6pase
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1,6-bisphosphatase
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liver-type
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splenectomy
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hk2
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dikinase
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glutaminolysis
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calprotectin
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triose
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shikonin
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2,3-diphosphoglycerate
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fructose-6-phosphate
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glycogenolysis
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drug development
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medicine
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biofuel production
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reticulocytosis
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transfusion-dependent
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spherocytosis
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nutrition
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diagnostics
- 2.7.1.40
- hexokinase
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phosphofructokinase
- erythrocyte
- fructose
- glucose-6-phosphate
- hepatocytes
- glycogen
- anemia
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carboxykinase
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gluconeogenesis
- aldolase
- pep
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hemolytic
- malate
- citrate
- creatine
- glucokinase
- adenylate
- carboxylase
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warburg
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gluconeogenic
- enolase
- phosphoglycerate
- pentose
- 6-phosphate
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malic
- glucagon
- glyceraldehyde-3-phosphate
- reticulocyte
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lipogenesis
- 6-phosphogluconate
- fructose-1,6-bisphosphate
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lipogenic
- 2,6-bisphosphate
- g6pase
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1,6-bisphosphatase
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liver-type
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splenectomy
- hk2
- dikinase
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glutaminolysis
-
calprotectin
- triose
- shikonin
- 2,3-diphosphoglycerate
- fructose-6-phosphate
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glycogenolysis
- drug development
- medicine
- biofuel production
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reticulocytosis
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transfusion-dependent
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spherocytosis
- nutrition
- diagnostics
Reaction
Synonyms
ATP/pyruvate O'-phosphotransferase, ATP:pyruvate 2-O-phosphotransferase, CPK, CPK1, cPK2, cPK3, cPK4, cPK5, CTHBP, cytosolic pyruvate kinase, cytosolic thyroid hormone binding protein, EHI_098420, EhPK, EhPyk, erythroid (R-type) pyruvate kinase, fluorokinase, hL-PYK, hLPYK, hPKM2, K+-dependent PK, K+-independent PK, kinase, fluoro- (phosphorylating), kinase, pyruvate (phosphorylating), L-PK
ECTree
2.7.1.40 pyruvate kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.40 - pyruvate kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C9S/C268S
C9S/C268S/K221C
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10000 times less active than the wild type enzyme
H425A
the A0.5 values for H425A are increased 8.0- and 60fold for D-ribose 5-phosphate and AMP
K221C
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10000 to 100000 times less active than the wild-type enzyme
K221D
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10000 to 100000 times less active than the wild-type enzyme
K221L
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10000 to 100000 times less active than the wild-type enzyme
K221R
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10000 to 100000 times less active than the wild-type enzyme
V435E
about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical
V435K
about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical
V435R
about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical
W416F/V435W
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high affinity for phosphoenolpyruvate compared to the wild-type enzyme, but its saturation curve is still sigmoidal and hyperbolic in the presence of allosteric activators
A137T
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increased instability, increased sensitivity to the allosteric inhibitor/product
C436A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436D
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436H
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436M
site-directed mutagenesis, crystal structure analysis, the mutant of L-PYK is the only residue 436 mutation that strengthens PEP affinity, revealing that the methionine substitution results in the ordering of several N-terminal residues that have not been ordered in previous structures
C436N
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436S
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436T
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
D499N
site-directed mutagenesis, the structure of the D499N mutant does not provide structural evidence for the previously observed allosteric activation of the D499N variant. The increase in PEP affinity observed for the D499N mutant in the absence of Fru-1,6-BP is due to the disruption of allosteric coupling across the C-C interface, crystal structure determination and analysis
F24A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
G415R
site-directed mutagenesis, the mutant binds fructose 1,6-bisphosphate, but is not activated by it, unlike the wild-type PKM2. But the mutant is activated by succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5'-phosphate (SAICAR)
H391Y
H464A
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site-directed mutagenesis of isozyme PKM2, the mutant shows no binding of and activation by serine
K367M
site-directed mutagenesis, the mutant lacks pyruvate kinase activity
K422R
K433E
the point mutant of PKM2 lacks phosphotyrosine peptide -binding ability
L16A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
L20A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
Q18A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
R479H
R510Q
S12A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
S12D
S437Y
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site-directed mutagenesis of isozyme PKM2, the mutant shows no binding of and activation by fructose 1,6-bisphosphate
S531E
site-directed mutagenesis, in the S531E variant glutamate binds in place of the 6'-phosphate of fructose-1,6-bisphosphate in the allosteric site, leading to partial allosteric activation, crystal structure determination and analysis
S531G
construction of mutant DELTA529/S531G, the mutant is not activated by Fru-1,6-BP, crystal structure determination and analysis
T22A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
W527H
site-directed mutagenesis, the increase in PEP affinity observed for the W527H mutant in the absence of Fru-1,6-BP is due to the disruption of allosteric coupling across the C-C interface, crystal structure determination and analysis
H480Q
site-directed mutagenesis of putative binding site of fructose 2,6-bisphosphate. Mutant displays hyperbolic kinetics that is not changed by addition of the allosteric effector fructose 2,6-bisphosphate
K453L
site-directed mutagenesis of putative binding site of fructose 2,6-bisphosphate. Mutant retains a sigmoidal kinetics and is little affected by addition of fructose 2,6-bisphosphate
K453L/H480Q
site-directed mutagenesis of putative binding sites of fructose 2,6-bisphosphate. Mutant displays hyperbolic kinetics
D315N
3.7% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.001 mM
D315S
1.4% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.00161 mM
E451W
72% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.000177 mM
K335R
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site-directed mutagenesis, structure compared to the wild-type, overview
S314N
69% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.000403 mM
S314Q
48% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.000122 mM
G338D
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loss-of-function mutation in the erythrocyte-specific pyruvate kinase gene resulting in hemolytic anemia with dramatic reduction in the half-life of eryhtrocytes. Mice carrying the mutation are highly resistant to infection with Plasmodium chabaudi. Mutation G338D has more severe effects on pyruvate kinase as well as higher protection against malaria infection than less severe mutation I90N
I90N
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loss-of-function mutation in the reythrocyte-specific pyruvate kinase gene, protective against blood-stage malaria. Mutation G338D has more severe effects on pyruvate kinase as well as higher protection against malaria infection than less severe mutation I90N
S240P
the mutant exhibits steady-state kinetic behavior that indicates that it is more responsive to regulation by effectors
W157A
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site-directed mutagenesis, Trp157 is located in domain B and close to the active site
W481A/W514A
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site-directed mutagenesis, Trp481 and Trp514 are located in domain C and close to the Y-interface
S22A
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mutant protein activity is decreased by as much as 90% when compared with wild-type, is more active in the absence of fructose 1,6-bisphosphate
T298A
T298C
T298S
S22A
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mutant protein activity is decreased by as much as 90% when compared with wild-type, is more active in the absence of fructose 1,6-bisphosphate
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F463V
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reduced affinity for fructose 1,6-diphosphate and fructose 2,6-diphosphate
R22G
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strongly reduced affinity for fructose 1,6-diphosphate and fructose 2,6-diphosphate
additional information
H391Y
pyruvate kinase M2 isozyme missense mutation found in cells from Bloom syndrome patients prone to develop cancer, the mutant protein maintains its homotetrameric structure, similar to the wild type protein, but shows a loss of activity of 20%, the mutant shows a 6fold increase in affinity for phosphoenolpyruvate and behaves like a non-allosteric protein with compromised cooperative binding
H391Y
naturally occuring mutation from a BS patient, mutation at intersubunit contact domain of the enzyme, the mutant shows 20% reduced activity compared to the wild-type enzyme, lost cooperativity and activation by fructose 1,6-bisphosphate, increased alpha-helical content, and 6fold increased PEP affinity
K422R
pyruvate kinase M2 isozyme missense mutation found in cells from Bloom syndrome patients prone to develop cancer, the mutant protein maintains its homotetrameric structure, similar to the wild type protein, but shows a loss of activity of 75%, the affinity for phosphoenolpyruvate is lost significantly in K422R
K422R
naturally occuring mutation at intersubunit contact domain of the enzyme, the mutant shows 75% reduced activity compared to the wild-type enzyme, 3fold reduced PEP affinity, and increased cooperativity
R510Q
similar kinetics as wild type, but dramatically decreased stability toward heat, more susceptible to ATP inhibition
R510Q
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increased instability, increased sensitivity to the allosteric inhibitor/product
S12D
site-directed mutagenesis, the S12D mutation mimics the effect of phosphorylation on L-PYK function, crystal structure analysis, overview
T298A
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mutation of the proton donor, mutant is enzymatically active, with decrease in kcat, Km, altered dissociation constants of ligands
T298A
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Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+
T298C
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no catalytic activity in the absence of the heterotrophic activator fructose 1,6-bisphosphate. In the presence of Mg2+ and D-fructose 1,6-bisphosphate, T298C has approximately 20% of the activity of wild-type enzyme. The activator constant for FBP increases by 1 order of magnitude compared to this constant with the wild type enzyme. T298C shows positive cooperativity by D-fructose 1,6-bisphosphate with a Hill coefficient of 2.6. Mn2+-activated T298C behaves like Mn2+-activated wild type enzyme with a Vmax that is 20% of that for the wild type enzyme with or without fructose-1,6-bisphosphate. A pH-rate profile of T298C relative to that for wild type enzyme shows that pKa2 has shifted from 6.4 in wild type to 5.5, indicating that the thiol group elicits an acidic pK shift. Inactivation of both wild type and T298C by iodoacetate elicits a pseudo-first-order loss of activity with T298C being inactivated from 8 to 100 times faster than wild-type enzyme. A pH dependence of the inactivation rate constant for T298C gives a value of pH 8.2, consistent with the pK for a thiol. Changes in fluorescence indicate that the T298C-Mg2+ complex binds PEP, ADP, and both ligands together. This demonstrates that the lack of activity is not due to the loss of substrate binding but to the lack of ability to induce the proper conformational change. The mutation also induces changes in binding of fructose-1,6-bisphosphate to all the relevant complexes. Binding of the metal and binding of phosphoenolpyruvate to the enzyme complexes are also differentially altered. Solvent isotope effects are observed for both wild type and T298C. Proton inventory studies indicate that kcat is affected by a proton from water in the transition state and the effects are metal ion-dependent. The results are consistent with water being the active site proton donor. Active site residue T298 is not critical for activity but plays a role in the activation of the water and affects the pK that modulates catalytic activity
T298C
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Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+
T298S
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mutation of the proton donor, mutant is enzymatically active, with decrease in kcat, Km, altered dissociation constants of ligands
T298S
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Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+
additional information
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the isopropyl-beta-D-thiogalactopyranoside-inducible pyk mutant produces 3fold higher levels of recombinant protein when grown on glucose as carbon source
additional information
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the isopropyl-beta-D-thiogalactopyranoside-inducible pyk mutant produces 3fold higher levels of recombinant protein when grown on glucose as carbon source
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additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
-
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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generation of W3110 derivative strains VH33, VH34 and VH35, that lack the main phosphoenolpyruvate consumers phosphoenolpyruvate:sugar phosphotransferase system and pyruvate kinase isozymes PykA and PykF causing modifications on cell physiology, carbon flux distribution and aromatics production capacity, overview. The phosphoenolpyruvate:sugar phosphotransferase-deficient strain shows lower specific rates for growth, glucose consumption and acetate production as well as a higher biomass yield from glucose. The effects are even more pronounced by the additional inactivation of PykA or PykF. The wild-type and mutant strains are modified to overproduce L-phenylalanine. In resting cells experiments, compared to reference strain, a 10, 4 and 7fold higher aromatics yields from glucose are observed as consequence of PTS, PTS PykA and PTS PykF inactivation, overview
additional information
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generation of W3110 derivative strains VH33, VH34 and VH35, that lack the main phosphoenolpyruvate consumers phosphoenolpyruvate:sugar phosphotransferase system and pyruvate kinase isozymes PykA and PykF causing modifications on cell physiology, carbon flux distribution and aromatics production capacity, overview. The phosphoenolpyruvate:sugar phosphotransferase-deficient strain shows lower specific rates for growth, glucose consumption and acetate production as well as a higher biomass yield from glucose. The effects are even more pronounced by the additional inactivation of PykA or PykF. The wild-type and mutant strains are modified to overproduce L-phenylalanine. In resting cells experiments, compared to reference strain, a 10, 4 and 7fold higher aromatics yields from glucose are observed as consequence of PTS, PTS PykA and PTS PykF inactivation, overview
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additional information
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contruction of stable transfectants of mouse SLC-3 cells with human pyruvate kinase cDNA. Expression of pyruvate kinase significantly decreases cells at the sub G0/G1 stage in an expression-level dependent manner. Pro-apoptotic genes such as Bad, Bnip3, and Bnip31, are down-regulated in the transfectants. Peroxiredoxin 1 and other antioxidant genes such as Cat, Txnrd1, and Glrx1 are also down-regulated
additional information
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overexpression of promyelocytic leukemia tumor suppressor protein mutant PML-2KA in the cytoplasm suppresses M2-type pyruvate kinase activity and the accumulation of lactate. PML-2KA suppresses the activity of the high-affinity terameric form of M2-type pyruvate kinase, but not of the low-affinity dimeric form
additional information
specific downregulation of M2-type pyruvate kinase by shRNA inhibits the replication of hepatitis C virus in hepatitis C virus replicon 9B cells
additional information
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G1168A and G1529A mutations at exon 11, as well as mutations C1492T, C1456T, G1291A, C1594T, G787A, G994A, and G1010C are associated with pyruvate kinase deficiency in south Iranian population
additional information
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construction of HCT116 cells silenced in both muscle isozymes PKM1 and PKM2, increased metabolic flux into the serine and glycine biosynthetic pathway in cells with reduced pyruvate kinase activity, serine and glycine deprivation decreases PKM2 activity in cells also influencing the glucose metabolism, overview
additional information
PKM2 knockout, retroviral production is used to generate HeLa S3 cells stably expressing shRNAs specific for PKM2 or AhR, and stable clones are selected with puromycin
additional information
molecular dynamics simulations are used to guide the design of mPKM2 internal light/oxygen/voltage-sensitive domain 2 (LOV2) fusion at position D24 (PiL[D24]), resulting in an engineered pyruvate kinase M2 (PKM2) variant that harbours an insertion of the light-sensing LOV2 domain from Avena Sativa within a region implicated in allosteric regulation by fructose 1,6-bisphosphate (FBP). The LOV2 photoreaction is preserved in the PiL[D24] chimera and causes secondary structure changes that are associated with a 30% decrease in the Km of the enzyme for phosphoenolpyruvate resulting in increased pyruvate kinase activity after light exposure. Importantly, this change in activity is reversible upon light withdrawal. Expression of PiL[D24] in cells leads to light-induced increase in labelling of pyruvate from glucose. Light induces a reversible increase in the enzymatic activity of purified PiL[D24]. Steady-state Michaelis-Menten kinetic parameters for PiL[D24] under dark and lit conditions determined by NMR spectroscopy at 21°C
additional information
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various N-terminal deletions and chimeric fusions to examine translocation signlaing mechanism
additional information
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construction of Htg- host strains carrying only one htg allele by repeatedly back crossing Htg- segregants from a hybrid between HB8-3A(Htg+) and BY4742(Htg-) to the Htg+ strain (HB8-3A). Three Htg strains with the desired genotype, designated HC1-5D, HE6-8D and HE120-12A, are successfully constructed by the repeated back crossing process, phenotypes, overview. The Htg+ CDC19-C allele leads to an increase in trehalose accumulation under heat stress conditions. Strains containing a single copy of the CDC19-C and CDC19-BY allele in the HE6-8D background exhibit increased trehalose accumulation under heat stress conditions. Nevertheless, replacement with a single copy of CDC19-C in the HE6-8D background does not contribute to a further increase in trehalose accumulation as compared with the HE6-8D strain carrying the Htg- CDC19-BY allele
additional information
construction of a C-terminally truncated mutant PKCT with a stop after residue 390. The catalytic activities of PKCT toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
additional information
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construction of a C-terminally truncated mutant PKCT with a stop after residue 390. The catalytic activities of PKCT toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
additional information
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construction of a C-terminally truncated mutant PKCT with a stop after residue 390. The catalytic activities of PKCT toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
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additional information
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overexpression of pyruvate kinase resulting in about fivefold increase in enzymic activity does not affect the growth rate or formate-to-lactate ratio significantly. Disruption of the gene encoding catabolite-control protein A results in a decrease in pyruvate kinase mRNA level
additional information
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recombinant overexpression of the enzyme in Clostridium thermocellum improves carbon flux to ethanol in the transformed cells. Clostridium thermocellum strain YD01 with exogenous pyruvate kinase, in which phosphoenolpyruvate carboxykinase expression is diminished by modifying the start codon from ATG to GTG, exhibits 3.25fold higher ethanol yield than the wild-type Clostridium thermocellum strain. A second strain, YD02 with exogenous pyruvate kinase, in which the gene for malic enzyme and part of malate dehydrogenase are deleted, has over 3fold higher ethanol yield than the wild-type strain
