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Literature summary for 2.7.11.2 extracted from
- Properties of the pyruvate dehydrogenase kinase bound to and separated from the dihydrolipoyl transacetylase-protein X subcomplex and evidence for binding of the kinase to protein X (1986), J. Biol. Chem., 261, 6515-6523.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dihydrolipoyl transacetylase | pyruvate dehydrogenase-complex transacetylase core | Bos taurus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | purified pyruvate dehydrogenase-complex contains 3 molecules of kinase, but one molecule of dihydrolipoyl transacetylase-protein x-subcomplex of pyruvate dehydrogenase activates more than 15 molecules of kinase | Bos taurus | 5739 | - |
| mitochondrion | protein x serves to anchor the kinase to the core of the complex | Bos taurus | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | requirement | Bos taurus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| kidney, from highly purifed pyruvate dehydrogenase-complex | Bos taurus |
| removed from the dihydrolipoyl transacetylase by treatment with p-hydroxymercuriphenylsulfonate | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | - |
Bos taurus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.018 | - |
purified dihydrolipoyl transacetylase-protein X-pyruvate dehydrogenase kinase subcomplex | Bos taurus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [pyruvate dehydrogenase (lipoamide)] | - |
Bos taurus | ADP + [pyruvate dehydrogenase (lipoamide)] phosphate | - |
ir | |
| 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 | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | subunit composition and complex structure | Bos taurus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Bos taurus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.512 | - |
ATP | - |
Bos taurus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Bos taurus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Bos taurus | |
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