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Literature summary for 2.3.1.12 extracted from
- Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1 (2003), Eur. J. Biochem., 270, 1050-1056.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Homo sapiens | |
| additional information | - |
additional information | - |
Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Homo sapiens | 5739 | - |
| mitochondrion | - |
Rattus norvegicus | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Homo sapiens |  |
| Mg2+ | - |
Rattus norvegicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | the enzyme mediates Ca2+-activation of isozymes 1 of pyruvate dehydrogenase phosphatase by 10fold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview | ? | - |
? | |
| additional information | Rattus norvegicus | the enzyme mediates Ca2+-activation of isozymes 1 of pyruvate dehydrogenase phosphatase by 10fold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
enzyme forms the core of the pyruvate dehydrogenase multienzyme complex | - |
| Rattus norvegicus | - |
enzyme forms the core of the pyruvate dehydrogenase multienzyme complex | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification of the multienzyme complex | Homo sapiens |
| purification of the multienzyme complex | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Rattus norvegicus | - |
| kidney | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme mediates Ca2+-activation of isozymes 1 of pyruvate dehydrogenase phosphatase by 10fold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview | Homo sapiens | ? | - |
? | |
| additional information | the enzyme mediates Ca2+-activation of isozymes 1 of pyruvate dehydrogenase phosphatase by 10fold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview | Rattus norvegicus | ? | - |
? | |
| additional information | interactions are different with the different isoforms of the regulatory enzymes of the multienzyme complex, signal mechanism for stimulation, overview, enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, the flexibly held outer domains of the enzyme show dynamic, E2 is responsible for effector-modified interactions with the complex' regulatory enzymes pyruvate dehydrogenase kinase PDK and pyruvate dehydrogenase phosphatase PDP, which exist in different isoforms, overview | Homo sapiens | ? | - |
? | |
| additional information | interactions are different with the different isoforms of the regulatory enzymes of the multienzyme complex, signal mechanism for stimulation, overview, enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, the flexibly held outer domains of the enzyme show dynamic, E2 is responsible for effector-modified interactions with the complex' regulatory enzymes pyruvate dehydrogenase kinase PDK and pyruvate dehydrogenase phosphatase PDP, which exist in different isoforms, overview | Rattus norvegicus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme forms the core unit E2, consisting of 4 domains in 60mer, a trimer of 3 20mers, of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase and dihydrolipoyl dehydrogenase, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview | Homo sapiens |
| More | the enzyme forms the core unit E2, consisting of 4 domains in 60mer, a trimer of 3 20mers, of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase and dihydrolipoyl dehydrogenase, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoyl acetyl transferase | - |
Homo sapiens |
| dihydrolipoyl acetyl transferase | - |
Rattus norvegicus |
| E2 | - |
Homo sapiens |
| More | the enzyme forms the core unit E2 of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview | Homo sapiens |
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Release 2023.1 (January 2023)
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