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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.025 | - |
ATP | pH 7.5, 30°C | Oryctolagus cuniculus |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
2000000 | - |
above 2000000, gel filtration | Oryctolagus cuniculus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
alpha-ketoacid dehydrogenase complex | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Oryctolagus cuniculus | - |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Oryctolagus cuniculus |
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 Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 8.3 | about half-maximal activity at pH 6.5 and 8.3 | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Calmodulin | activation | Oryctolagus cuniculus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.13 | - |
ADP | pH 7.5, 30°C | Oryctolagus cuniculus |