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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

Reaction

ATP
+
pyruvate
=
ADP
+
phosphoenolpyruvate

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 , L-PYK, liver PK, liver pyruvate kinase, M1-PK, M1-PYK, M2 pyruvate kinase, M2 type phosphoenolpyruvate kinase, M2-PK, M2-pyruvate kinase, M2-type pyruvate kinase, M2PK, mPKM2, MRSA PK, muscle PK, NCgl2008, NCgl2809, PAE0819, PfPYK, pfPyrK, phosphoenol transphosphorylase, phosphoenolpyruvate kinase, phosphoenolpyruvate: ADP phosphotransferase, PK-alphabeta1, PK-alphabeta2, PK-M1, PK-M2, PK-R, PK-S, PK1, PK3, PKC, PKC1, PKL, Pklr, PKM1, PKM2, PKp, ProTalphaK, PYK, PYK-I, Pyk1, Pyk2, PykA, PykF, PyKII, pyruvate kinase, pyruvate kinase 1, pyruvate kinase isoenzyme M2, pyruvate kinase isoform M2, pyruvate kinase isoforms 2, pyruvate kinase isozyme M1, pyruvate kinase isozyme type M2, pyruvate kinase M1, pyruvate kinase M2, pyruvate kinase M2 isoform, pyruvate kinase muscle isoform 2, pyruvate kinase muscle isozyme, pyruvate kinase type M2, pyruvate kinase type-II, pyruvate phosphotransferase, pyruvic kinase, R-type pyruvate kinase, R-type/L-type pyruvate kinase, red cell/liver pyruvate kinase, rM1-PYK, RMPK, RPK, Rv1617, SSO0981, TbrPYK, TCIL3000_10_12020, TcoPYK, THBP1, TuM2-PK, tumor cell specific pyruvate kinase isozyme M2, tumour M2-PK, tumour M2-pyruvate kinase, VcIIPK, VcIPK, VC_0485, VC_2008, VEG17, vegetative protein 17, vesicle-associated pyruvate kinase, YPK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.40 pyruvate kinase

Temperature Stability

Temperature Stability on EC 2.7.1.40 - pyruvate kinase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105
thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of this hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability
110
-
half-life: 30 min. (NH4)2SO4, NaCl or KCl, each at 1 mM, do not stabilize the enzyme agianst heat inactivation
20
-
most stable at
20 - 70
enzyme EhPyk thermal denaturation study at different pH values, overview
25 - 75
-
more than 60% activity between 25 and 75°C, the enzyme retains 80% of its activity after 2 min at 75°C
30
-
up to, in 50 mM HEPES-potassium hydroxide buffer, pH 7.5, 0.1 M mercaptoethanol, 20% v/v glycerol, 30 min stable
4
the wild type enzyme and mutant enzyme K422R shows complete loss of activity after 15 min at 4°C, the mutant enzyme H391Y shows 36% loss of activity after 15 min at 4°C
50 - 52
-
50% loss of activity after 10 min at 50-52°C
50 - 55
-
completely inactivated after 3 min of incubation at 50 to 55°C
58 - 63
-
58% loss of activity after 10 min at 58-63°C
80
-
sensitive to heat at 80°C
99
thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of the hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability
additional information