EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.2 | 2-oxoisopentanoate | - |
Bos taurus | |
2.7.11.2 | acetyl-CoA | - |
Bos taurus | |
2.7.11.2 | dihydrolipoyl transacetylase | 3-5fold stimulation | Bos taurus | |
2.7.11.2 | NADH | activation, in the presence of NH4+ | Bos taurus | |
2.7.11.2 | NADH | activation, in the presence of K+ | Bos taurus |
EC Number | General Stability | Organism |
---|---|---|
2.7.11.2 | kinase has tendency to aggregate in other buffers than 0.01 M imidazole-asparagine, pH 7.3, 0.1 mM MgCl2, 0.01 M EDTA | Bos taurus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.2 | ADP | competitive to ATP; inhibition only in the presence of monovalent cations | Bos taurus | |
2.7.11.2 | additional information | no inhibition by cAMP; no inhibition by cGMP | Bos taurus | |
2.7.11.2 | pyruvate | synergism with ADP | Bos taurus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.11.2 | 0.0006 | - |
[pyruvate dehydrogenase (acetyl-transferring)] | pH 7.0, 30°C | Bos taurus | |
2.7.11.2 | 0.0006 | - |
[pyruvate dehydrogenase (acetyl-transferring)] | in presence of dihydrolipoyl transacetylase | Bos taurus | |
2.7.11.2 | 0.02 | - |
ATP | kidney enzyme | Bos taurus | |
2.7.11.2 | 0.02 | - |
Mg2+ | kidney enzyme | Bos taurus | |
2.7.11.2 | 0.02 | - |
ATP | pH 7.0, 30°C | Bos taurus | |
2.7.11.2 | 0.02 | - |
Mg2+ | pH 7.0, 30°C | Bos taurus | |
2.7.11.2 | 0.02 | - |
[pyruvate dehydrogenase (acetyl-transferring)] | pH 7.0, 30°C | Bos taurus | |
2.7.11.2 | 0.02 | - |
[pyruvate dehydrogenase (acetyl-transferring)] | in absence of dihydrolipoyl transacetylase | Bos taurus | |
2.7.11.2 | 0.02 | - |
ATP | pyruvate dehydrogenase complex | Bos taurus | |
2.7.11.2 | 0.02 | - |
Mg2+ | pyruvate dehydrogenase complex | Bos taurus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.7.11.2 | mitochondrion | tightly bound to dihydrolipoamide acetyltransferase of pyruvate dehydrogenase complex | Bos taurus | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.2 | Mg2+ | requirement | Bos taurus | |
2.7.11.2 | Mg2+ | actual substrate: MgATP2- | Bos taurus | |
2.7.11.2 | Mn2+ | requirement | Bos taurus | |
2.7.11.2 | Mn2+ | can replace Mg2+ to some extent | Bos taurus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.7.11.2 | 45000 | - |
1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE | Bos taurus |
2.7.11.2 | 48000 | - |
1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE | Bos taurus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.11.2 | ATP + [pyruvate dehydrogenase (lipoamide)] | Bos taurus | catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 | ADP + [pyruvate dehydrogenase (lipoamide)] phosphate | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.11.2 | Bos taurus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.11.2 | kidney, from highly purifed pyruvate dehydrogenase-complex | Bos taurus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.7.11.2 | heart | - |
Bos taurus | - |
2.7.11.2 | kidney | - |
Bos taurus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.11.2 | 0.332 | - |
purified enzyme, in presence of dihydrolipoyl transacetylase | Bos taurus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.11.2 | ATP + [pyruvate dehydrogenase (acetyl-transferring)] | - |
Bos taurus | ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate | - |
? | |
2.7.11.2 | ATP + [pyruvate dehydrogenase (lipoamide)] | highly specific for the substrate | Bos taurus | ADP + [pyruvate dehydrogenase (lipoamide)] phosphate | - |
ir | |
2.7.11.2 | ATP + [pyruvate dehydrogenase (lipoamide)] | incorporates gamma-phosphate from ATP into E1-component of pyruvate dehydrogenase-complex alpha-subunit | Bos taurus | ADP + [pyruvate dehydrogenase (lipoamide)] phosphate | - |
ir | |
2.7.11.2 | ATP + [pyruvate dehydrogenase (lipoamide)] | phosphorylation sites are 3 Ser-residues in the alpha-subunit, i.e. E1, MW 41000, of pyruvate dehydrogenase | Bos taurus | ADP + [pyruvate dehydrogenase (lipoamide)] phosphate | - |
ir | |
2.7.11.2 | ATP + [pyruvate dehydrogenase (lipoamide)] | catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 | Bos taurus | ADP + [pyruvate dehydrogenase (lipoamide)] phosphate | - |
ir | |
2.7.11.2 | additional information | no activity with glycogen synthase a and rabbit skeletal muscle phosphorylase b | Bos taurus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.11.2 | dimer | 1 * 48000, alpha + 1 * 45000, beta, SDS-PAGE | Bos taurus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.11.2 | 30 | - |
assay at | Bos taurus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.11.2 | 7 | - |
assay at | Bos taurus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.2 | ATP | dependent on | Bos taurus | |
2.7.11.2 | additional information | no activation by cAMP | Bos taurus | |
2.7.11.2 | additional information | no activation by cGMP | Bos taurus |