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Literature summary for 1.2.1.104 extracted from
- Interactions of the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus (2003), Eur. J. Biochem., 270, 4488-4496.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| M131A | mutation in the peripheral subunit-binding domain of the E2 chain. Residue M131 makes a significant contribution to the binding of pyruvate decarboxylase E1. Mutation lowers the binding affinity for pyruvate decarboxylase E1 by almost 140fold | Geobacillus stearothermophilus |
| additional information | residues K136, K153, R146, S133 do not contribute to the interaction with pyruvate decarboxylase E1 | Geobacillus stearothermophilus |
| R135A | mutation in the peripheral subunit-binding domain of the E2 chain, lowers the binding affinity for pyruvate decarboxylase E1 by almost 140fold | Geobacillus stearothermophilus |
| R135C | mutation in the peripheral subunit-binding domain of the E2 chain, plays an important part in the interaction with both pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3 | Geobacillus stearothermophilus |
| R135K | mutant behaves almost like the wild-type | Geobacillus stearothermophilus |
| R156A | mutation in the peripheral subunit-binding domain of the E2 chain, lowers the binding affinity for pyruvate decarboxylase E1 by almost 19fold | Geobacillus stearothermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Geobacillus stearothermophilus | - |
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Release 2023.1 (January 2023)
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