EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.2.4.4 | thiamine diphosphate | - |
Oryctolagus cuniculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.4 | ADP | kinetics | Oryctolagus cuniculus | |
2.7.11.4 | Ca2+ | - |
Oryctolagus cuniculus | |
2.7.11.4 | Dichloroacetate | ATP slightly protects | Oryctolagus cuniculus | |
2.7.11.4 | additional information | no inhibition by GTP | Oryctolagus cuniculus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.4.4 | 0.014 | - |
3-methyl-2-oxopentanoate | - |
Oryctolagus cuniculus | |
1.2.4.4 | 0.015 | - |
4-methyl-2-oxopentanoate | - |
Oryctolagus cuniculus | |
1.2.4.4 | 0.028 | - |
3-methyl-2-oxobutanoate | - |
Oryctolagus cuniculus | |
1.2.4.4 | 0.715 | - |
pyruvate | - |
Oryctolagus cuniculus | |
2.7.11.4 | 0.025 | - |
ATP | pH 7.5, 30°C | Oryctolagus cuniculus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.4 | EGTA | 0.1 mM | Oryctolagus cuniculus | |
2.7.11.4 | Mg2+ | requirement, actual substrate: MgATP2- | Oryctolagus cuniculus | |
2.7.11.4 | Mg2+ | Km-value: 0.025 mM | Oryctolagus cuniculus | |
2.7.11.4 | additional information | no activation by Ca2+ | Oryctolagus cuniculus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.2.4.4 | additional information | - |
MW of the multienzyme complex is 2000000 Da, determined by gel filtration | Oryctolagus cuniculus |
2.7.11.4 | 2000000 | - |
above 2000000, gel filtration | Oryctolagus cuniculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.4.4 | additional information | Oryctolagus cuniculus | regulation by phosphorylation-dephosphorylation | ? | - |
? | |
2.7.11.4 | ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | Oryctolagus cuniculus | phosphorylation inactivates EC 1.2.4.4 | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.4.4 | Oryctolagus cuniculus | - |
- |
- |
2.7.11.4 | Oryctolagus cuniculus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.4.4 | multienzyme complex | Oryctolagus cuniculus |
2.7.11.4 | alpha-ketoacid dehydrogenase complex | Oryctolagus cuniculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.2.4.4 | liver | - |
Oryctolagus cuniculus | - |
2.7.11.4 | liver | - |
Oryctolagus cuniculus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.2.4.4 | 3.2 | - |
- |
Oryctolagus cuniculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.4.4 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine | - |
Oryctolagus cuniculus | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 | - |
? | |
1.2.4.4 | 3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine | - |
Oryctolagus cuniculus | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2 | - |
? | |
1.2.4.4 | 4-methyl-2-oxopentanoate + NAD+ + CoA | - |
Oryctolagus cuniculus | 3-methylbutanoyl-CoA + CO2 + NADH | - |
? | |
1.2.4.4 | additional information | regulation by phosphorylation-dephosphorylation | Oryctolagus cuniculus | ? | - |
? | |
1.2.4.4 | pyruvate + NAD+ + CoA | - |
Oryctolagus cuniculus | acetyl-CoA + CO2 + NADH | - |
? | |
2.7.11.4 | ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | GTP cannot replace ATP | Oryctolagus cuniculus | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? | |
2.7.11.4 | ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | phosphorylates exclusively MW 47000 subunit of substrate | Oryctolagus cuniculus | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? | |
2.7.11.4 | ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] | phosphorylation inactivates EC 1.2.4.4 | Oryctolagus cuniculus | ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.11.4 | 37 | - |
assay at | Oryctolagus cuniculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.11.4 | additional information | - |
HEPES-potassium buffer promotes higher activity than imidazole-chloride, 4-morpholinopropanesulfonic acid-potassium or potassium phosphate buffer | Oryctolagus cuniculus |
2.7.11.4 | 7.1 | - |
- |
Oryctolagus cuniculus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.7.11.4 | 6.5 | 8.3 | about half-maximal activity at pH 6.5 and 8.3 | Oryctolagus cuniculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.4.4 | CoA | - |
Oryctolagus cuniculus | |
1.2.4.4 | NAD+ | - |
Oryctolagus cuniculus | |
2.7.11.4 | Calmodulin | activation | Oryctolagus cuniculus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.11.4 | 0.13 | - |
ADP | pH 7.5, 30°C | Oryctolagus cuniculus |