Protein Variants | Comment | Organism |
---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
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 | |
Dichloroacetate | binding kinetics | Homo sapiens | |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
isozyme PDHK2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Comment | Organism |
---|---|---|
dimer or tetramer | effects of ligand binding on distal structure of PDHK2, analytical ultracentrifugation, structure, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
PDHK | - |
Homo sapiens |
pyruvate dehydrogenase kinase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 |