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Literature summary extracted from

  • Hiromasa, Y.; Hu, L.; Roche, T.E.
    Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2 (2006), J. Biol. Chem., 281, 12568-12579.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.2 W383F site-directed mutagenesis of isozyme PDHK2, the mutant shows unaltered catalytic activity compared to the wild-type isozyme PDHK2, but altered ligand binding and higher sensitivity to inhibition by pyruvate and ADP Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.2 ADP binding kinetics,ATP or ADP plus pyruvate at low concentration of about 0.1 mM cause PDHK2 dimer to associate to a tetramer. These changes make major contributions to synergistic inhibition of PDHK2 activity by ADP and pyruvate, overview Homo sapiens
2.7.11.2 Dichloroacetate binding kinetics Homo sapiens
2.7.11.2 pyruvate binding kinetics,ATP or ADP plus pyruvate at low concentration of about 0.1 mM cause PDHK2 dimer to associate to a tetramer. These changes make major contributions to synergistic inhibition of PDHK2 activity by ADP and pyruvate, overview Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.2 additional information Homo sapiens PDHK2 is required for binding to the inner lipoyl domain L2 of the dihydrolipoyl acetyltransferase of the pyruvate dehydrogenase complex ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.12 Homo sapiens
-
-
-
2.7.11.2 Homo sapiens
-
 isozyme PDHK2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.2 additional information PDHK2 is required for binding to the inner lipoyl domain L2 of the dihydrolipoyl acetyltransferase of the pyruvate dehydrogenase complex Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.11.2 dimer or tetramer effects of ligand binding on distal structure of PDHK2, analytical ultracentrifugation, structure, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.3.1.12 dihydrolipoyl acetyltransferase component E2
-
 Homo sapiens
2.7.11.2 PDHK
-
 Homo sapiens
2.7.11.2 pyruvate dehydrogenase kinase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.2 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.2 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.2 ATP binding kinetics, ATP or ADP plus pyruvate at low concentration of about 0.1 mM cause PDHK2 dimer to associate to a tetramer. These changes make major contributions to synergistic inhibition of PDHK2 activity by ADP and pyruvate, overview Homo sapiens