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Literature summary for 2.7.11.4 extracted from
- Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation (1982), J. Biol. Chem., 257, 14433-14439.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP | kinetics | Oryctolagus cuniculus |  |
| Ca2+ | - |
Oryctolagus cuniculus | |
| Dichloroacetate | ATP slightly protects | Oryctolagus cuniculus | |
| additional information | no inhibition by GTP | Oryctolagus cuniculus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.025 | - |
ATP | pH 7.5, 30°C | Oryctolagus cuniculus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| EGTA | 0.1 mM | Oryctolagus cuniculus | |
| Mg2+ | requirement, actual substrate: MgATP2- | Oryctolagus cuniculus | |
| Mg2+ | Km-value: 0.025 mM | Oryctolagus cuniculus | |
| additional information | no activation by Ca2+ | Oryctolagus cuniculus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 2000000 | - |
above 2000000, gel filtration | Oryctolagus cuniculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | Oryctolagus cuniculus | phosphorylation inactivates EC 1.2.4.4 | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| alpha-ketoacid dehydrogenase complex | Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | GTP cannot replace ATP | Oryctolagus cuniculus | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? | |
| ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | phosphorylates exclusively MW 47000 subunit of substrate | Oryctolagus cuniculus | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? | |
| ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | phosphorylation inactivates EC 1.2.4.4 | Oryctolagus cuniculus | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
HEPES-potassium buffer promotes higher activity than imidazole-chloride, 4-morpholinopropanesulfonic acid-potassium or potassium phosphate buffer | Oryctolagus cuniculus |
| 7.1 | - |
- |
Oryctolagus cuniculus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 8.3 | about half-maximal activity at pH 6.5 and 8.3 | Oryctolagus cuniculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Calmodulin | activation | Oryctolagus cuniculus | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.13 | - |
ADP | pH 7.5, 30°C | Oryctolagus cuniculus | |
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