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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.7.11.2 2-oxoisopentanoate
-
Bos taurus
2.7.11.2 acetyl-CoA
-
Bos taurus
2.7.11.2 dihydrolipoyl transacetylase 3-5fold stimulation Bos taurus
2.7.11.2 NADH activation, in the presence of NH4+ Bos taurus
2.7.11.2 NADH activation, in the presence of K+ Bos taurus

General Stability

EC Number General Stability Organism
2.7.11.2 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.2 0.0006
-
[pyruvate dehydrogenase (acetyl-transferring)] pH 7.0, 30°C Bos taurus
2.7.11.2 0.0006
-
[pyruvate dehydrogenase (acetyl-transferring)] in presence of dihydrolipoyl transacetylase Bos taurus
2.7.11.2 0.02
-
ATP kidney enzyme Bos taurus
2.7.11.2 0.02
-
Mg2+ kidney enzyme Bos taurus
2.7.11.2 0.02
-
ATP pH 7.0, 30°C Bos taurus
2.7.11.2 0.02
-
Mg2+ pH 7.0, 30°C Bos taurus
2.7.11.2 0.02
-
[pyruvate dehydrogenase (acetyl-transferring)] pH 7.0, 30°C Bos taurus
2.7.11.2 0.02
-
[pyruvate dehydrogenase (acetyl-transferring)] in absence of dihydrolipoyl transacetylase Bos taurus
2.7.11.2 0.02
-
ATP pyruvate dehydrogenase complex Bos taurus
2.7.11.2 0.02
-
Mg2+ pyruvate dehydrogenase complex Bos taurus

Localization

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.11.2 45000
-
1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE Bos taurus
2.7.11.2 48000
-
1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.2 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

EC Number Organism UniProt Comment Textmining
2.7.11.2 Bos taurus
-
-
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.2 heart
-
Bos taurus
-
2.7.11.2 kidney
-
Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.11.2 0.332
-
purified enzyme, in presence of dihydrolipoyl transacetylase Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.2 ATP + [pyruvate dehydrogenase (acetyl-transferring)]
-
Bos taurus ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
-
?
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] highly specific for the substrate Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
2.7.11.2 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
2.7.11.2 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
2.7.11.2 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
2.7.11.2 additional information no activity with glycogen synthase a and rabbit skeletal muscle phosphorylase b Bos taurus ?
-
?

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.2 30
-
assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.2 7
-
assay at Bos taurus

Cofactor

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