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Literature summary extracted from

  • Pawelczyk, T.; Olson, M.S.
    Regulation of pyruvate dehydrogenase kinase activity from pig kidney cortex (1992), Biochem. J., 288, 369-373.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.2 Cl- 40% inhibition at 80 mM, K+-independent inhibition Sus scrofa
2.7.11.2 HPO42- noncompetitive to ATP in the range of 1-10 mM; within physiological range, only in the presence of K+, not in its absence Sus scrofa
2.7.11.2 additional information increase of ionic strength inhibits, changes of osmolarity of assay medium do not affect activity Sus scrofa
2.7.11.2 SO42- with the same effect as HPO42- Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.2 additional information
-
 additional information changes in ionic strength Sus scrofa
2.7.11.2 0.01
-
 ATP at 0.2 M buffer concentration Sus scrofa
2.7.11.2 0.025
-
 ATP at 0.04 M buffer concentration Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.2 K+ 2.2fold activation at 20 mM K+, not pH- and buffer concentration-dependent Sus scrofa
2.7.11.2 Mg2+ requirement Sus scrofa
2.7.11.2 additional information no activation by Na+ Sus scrofa

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)] Sus scrofa 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 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.2 kidney cortex Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] optimum activity within a small range of ionic strength of 0.03-0.05 M Sus scrofa 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 Sus scrofa ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.2 additional information
-
 optimal activity within a range of 0.03 M and 0.05 M buffer concentrations Sus scrofa
2.7.11.2 7.2 8 broad, at 0.15 M buffer concentration Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.11.2 6.2 9 about half-maximal activity at pH 6.2 and 9 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.2 ATP dependent on Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.11.2 10
-
 HPO42- pH 7.8, 30°C Sus scrofa