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Literature summary for 2.3.1.12 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of truncated thrombin-cleavable enzyme in Escherichia coli strain BL21(DE3) | Geobacillus stearothermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K136A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| K153A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| M131A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R135A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R135C | site-directed mutagenesis, additional alkylation of the mutant enzymes with methyl, ethyl, propyl and butyl groups, the modifications cause alterations in interaction of core unit, E1 and E3 in the enzyme complex compared to the wild-type complex, thermodynamics and kinetics in comparison to the wild-type enzyme, overview | Geobacillus stearothermophilus |
| R135K | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R135L | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R135M | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R139A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R146A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| R156A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
| S133A | site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme | Geobacillus stearothermophilus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the complex assembly and maintainance is regulated by thermodynamic homeostasis or entropy-enthalpy compensation | Geobacillus stearothermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Geobacillus stearothermophilus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme forms the core unit of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its peripheral domain, Arg135 is important for interactions with E1 and E3, Met131 is involved in binding of E1, interaction analysis by surface plasmon resonance | Geobacillus stearothermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoyl acetyltransferase | - |
Geobacillus stearothermophilus |
| E2 | - |
Geobacillus stearothermophilus |
| More | the enzyme forms the core unit E2 of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase and dihydrolipoyl dehydrogenase, tightly at its peripheral domain | Geobacillus stearothermophilus |
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Release 2023.1 (January 2023)
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