Cloned (Comment) | Organism |
---|---|
expression of the enzymes' L2 domain as GST-fusion protein | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | complex component interactions among each other and with regulatory enzyme pyruvate dehydrogenase kinase isozyme 2, overview, dissociation constants of interaction of L2 and recombinant GST-L2 with PDK isozyme 2, reduced PDK2 binding to E2-E1, reversible bifunctional binding to L2 with the mandatory singly held transition fits the proposed 'hand-over-hand' movement of a kinase dimer to access E1 without dissociating from the complex | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | the enzyme E2 has an enormous impact on pyruvate dehydrogenase kinase PDK phosphorylation of the pyruvate dehydrogenase E1 component by acting as a mobile binding framework and in facilitating and mediating regulation of PDK activity, isozyme PDK2 interacts very weakly with L2 domain of E2, but much tighter with the recombinant dimeric glutathione S-transferase-L2 domain fusion protein, importance of bifunctional binding, interaction of PDK2 with the lipoyl domains L1 and L2 of E2, and the E3-binding protein L3, overview | ? | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme E2 has an enormous impact on pyruvate dehydrogenase kinase PDK phosphorylation of the pyruvate dehydrogenase E1 component by acting as a mobile binding framework and in facilitating and mediating regulation of PDK activity, isozyme PDK2 interacts very weakly with L2 domain of E2, but much tighter with the recombinant dimeric glutathione S-transferase-L2 domain fusion protein, importance of bifunctional binding, interaction of PDK2 with the lipoyl domains L1 and L2 of E2, and the E3-binding protein L3, overview | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 60mer, analytical ultracentrifugation | Homo sapiens |
More | E2 is composed of 4 domains including the innerlipoyl domain L2 important for binding of E1 | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
dihydrolipoyl acetyltransferase | - |
Homo sapiens |
E2 | - |
Homo sapiens |
More | the enzyme forms the core unit E2 of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview | Homo sapiens |