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Literature summary for 2.7.11.2 extracted from

  • Pettit, F.H.; Yeaman, S.J.; Reed, L.J.
    Pyruvate dehydrogenase kinase from bovine kidney (1982), Methods Enzymol., 90, 195-201.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
2-oxoisopentanoate
-
Bos taurus
acetyl-CoA
-
Bos taurus
dihydrolipoyl transacetylase 3-5fold stimulation Bos taurus
NADH activation, in the presence of NH4+ Bos taurus
NADH activation, in the presence of K+ Bos taurus

General Stability

General Stability Organism
kinase has tendency to aggregate in other buffers than 0.01 M imidazole-asparagine, pH 7.3, 0.1 mM MgCl2, 0.01 M EDTA Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ADP competitive to ATP; inhibition only in the presence of monovalent cations Bos taurus
additional information no inhibition by cAMP; no inhibition by cGMP Bos taurus
pyruvate synergism with ADP Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0006
-
[pyruvate dehydrogenase (acetyl-transferring)] pH 7.0, 30°C Bos taurus
0.0006
-
[pyruvate dehydrogenase (acetyl-transferring)] in presence of dihydrolipoyl transacetylase Bos taurus
0.02
-
ATP kidney enzyme Bos taurus
0.02
-
Mg2+ kidney enzyme Bos taurus
0.02
-
ATP pH 7.0, 30°C Bos taurus
0.02
-
Mg2+ pH 7.0, 30°C Bos taurus
0.02
-
[pyruvate dehydrogenase (acetyl-transferring)] pH 7.0, 30°C Bos taurus
0.02
-
[pyruvate dehydrogenase (acetyl-transferring)] in absence of dihydrolipoyl transacetylase Bos taurus
0.02
-
ATP pyruvate dehydrogenase complex Bos taurus
0.02
-
Mg2+ pyruvate dehydrogenase complex Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion tightly bound to dihydrolipoamide acetyltransferase of pyruvate dehydrogenase complex Bos taurus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Bos taurus
Mg2+ actual substrate: MgATP2- Bos taurus
Mn2+ requirement Bos taurus
Mn2+ can replace Mg2+ to some extent Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE Bos taurus
48000
-
1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [pyruvate dehydrogenase (lipoamide)] Bos taurus catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
kidney, from highly purifed pyruvate dehydrogenase-complex Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-
kidney
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.332
-
purified enzyme, in presence of dihydrolipoyl transacetylase Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [pyruvate dehydrogenase (acetyl-transferring)]
-
Bos taurus ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
-
?
ATP + [pyruvate dehydrogenase (lipoamide)] highly specific for the substrate Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
ATP + [pyruvate dehydrogenase (lipoamide)] incorporates gamma-phosphate from ATP into E1-component of pyruvate dehydrogenase-complex alpha-subunit Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
ATP + [pyruvate dehydrogenase (lipoamide)] phosphorylation sites are 3 Ser-residues in the alpha-subunit, i.e. E1, MW 41000, of pyruvate dehydrogenase Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
additional information no activity with glycogen synthase a and rabbit skeletal muscle phosphorylase b Bos taurus ?
-
?

Subunits

Subunits Comment Organism
dimer 1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Bos taurus
additional information no activation by cAMP Bos taurus
additional information no activation by cGMP Bos taurus