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Literature summary for 2.7.11.2 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
Search for more literature for 2.7.11.2

Inhibitors

Inhibitors Comment Organism Structure
Cl- 40% inhibition at 80 mM, K+-independent inhibition Sus scrofa
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
additional information increase of ionic strength inhibits, changes of osmolarity of assay medium do not affect activity Sus scrofa
SO42- with the same effect as HPO42- Sus scrofa

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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]

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

pH Optimum

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

pH Range

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

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Sus scrofa

Ki Value [mM]

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