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Literature summary for 2.3.1.12 extracted from
- Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase (2003), J. Biol. Chem., 278, 33681-33693.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the enzymes' L2 domain as GST-fusion protein | Homo sapiens |
KM Value [mM]
| 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/ Products (Substrates)
| 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 | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| 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
| 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
| 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 |
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