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Literature summary for 2.3.1.12 extracted from
- Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex (2008), FEBS Lett., 582, 468-472.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| a recombinant fragment hL2S (containing the second lipoyl domain (L2), second hinge region, E1-binding domain (S) and third hinge region of hE2, residues 128330) is overexpressed in Escherichia coli | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K276A | mutant shows negligible binding to human pyruvate dehydrogenase with 86fold higher KD compared to wild-type | Homo sapiens |
| R297A | mutant is found to have KD 6.8fold higher than that for the wild-type, indicating a possible involvement of this residue in the interaction with human pyruvate dehydrogenase, but not with the C-terminal residue of beta-subunit | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2) | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-nitrilotriacetate-agarose affinity chromatography | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2) | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoyl acetyltransferase | - |
Homo sapiens |
| hE2 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). K276 of hE2 is involved in the interaction with pyruvate dehydrogenase | Homo sapiens |
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Release 2023.1 (January 2023)
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