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Literature summary for 2.7.11.2 extracted from

  • Kerbey, A.L.; Randle, P.J.
    Pyruvate dehydrogenase kinase activity of pig heart pyruvate dehydrogenase (E1 component of pyruvate dehydrogenase complex) (1985), Biochem. J., 231, 523-529.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
dihydrolipoyl transacetylase
-
Bos taurus
dihydrolipoyl transacetylase rate-limiting in the holo-complex Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
pyruvate
-
Bos taurus
pyruvate
-
Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Sus scrofa 5739
-
mitochondrion
-
Bos taurus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Sus scrofa
Mg2+ requirement Bos taurus
Mg2+ actual substrate: MgATP2- Sus scrofa
Mg2+ actual substrate: MgATP2- Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
136000
-
pyruvate dehydrogenase, gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

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

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa
kidney, from highly purifed pyruvate dehydrogenase-complex Bos taurus
removed from the dihydrolipoyl transacetylase by treatment with p-hydroxymercuriphenylsulfonate Bos taurus

Source Tissue

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.9 2.7 purified enzyme, in presence of dihydrolipoyl transacetylase, reconstituted enzyme complex Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [pyruvate dehydrogenase (lipoamide)] incorporates gamma-phosphate from ATP into E1-component of pyruvate dehydrogenase-complex alpha-subunit Sus scrofa 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)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Sus scrofa 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

Subunits

Subunits Comment Organism
More subunit composition and complex structure Sus scrofa
More subunit composition and complex structure Bos taurus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Sus scrofa
ATP dependent on Bos taurus