Protein Variants | Comment | Organism |
---|---|---|
E182A | binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered | Homo sapiens |
E182Q | binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered | Homo sapiens |
additional information | construction of diverse L2 domain mutants, e.g. substitutions of A172, D173, Leu140, Glu162, Glu181, and Glu179 highly reduce binding of L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 | Homo sapiens |
V180S/E181L | binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | starvation inhibits the overall complex reaction | Homo sapiens | |
additional information | starvation inhibits the overall complex reaction | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | binding constants of multienzyme complex components and regulatory enzymes, overview | Homo sapiens | |
additional information | - |
additional information | binding constants of multienzyme complex components and regulatory enzymes, overview | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
mitochondrion | - |
Rattus norvegicus | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Homo sapiens | |
Mg2+ | - |
Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | E2 plays a central role in organization, integrated chemical reactions, and regulation of the multienzyme complex, overview, binding and activation of regulatory enzyme pyruvate dehydrogenase kinase isozymes PDK1-4, the enzyme mediates Ca2+-activation of isozymes of pyruvate dehydrogenase phosphatase severalfold, 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 | E2 plays a central role in organization, integrated chemical reactions, and regulation of the multienzyme complex, overview, binding and activation of regulatory enzyme pyruvate dehydrogenase kinase isozymes PDK1-4, the enzyme mediates Ca2+-activation of isozymes of pyruvate dehydrogenase phosphatase severalfold, 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | E2 plays a central role in organization, integrated chemical reactions, and regulation of the multienzyme complex, overview, binding and activation of regulatory enzyme pyruvate dehydrogenase kinase isozymes PDK1-4, the enzyme mediates Ca2+-activation of isozymes of pyruvate dehydrogenase phosphatase severalfold, 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 | E2 plays a central role in organization, integrated chemical reactions, and regulation of the multienzyme complex, overview, binding and activation of regulatory enzyme pyruvate dehydrogenase kinase isozymes PDK1-4, the enzyme mediates Ca2+-activation of isozymes of pyruvate dehydrogenase phosphatase severalfold, 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 | the overall complex reaction is irreversible | Homo sapiens | ? | - |
? | |
additional information | the overall complex reaction is irreversible | Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme is a 60mer, E2 domain structure: 4 domains, i.e. L1, L2, B, and I domain, connected by linker oligomers, overview, overall multienzyme complex organization, overview | Homo sapiens |
More | enzyme is a 60mer, E2 domain structure: 4 domains, i.e. L1, L2, B, and I domain, connected by linker oligomers, overview, overall multienzyme complex organization, overview | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
dihydrolipoyl acetyltransferase | - |
Homo sapiens |
dihydrolipoyl acetyltransferase | - |
Rattus norvegicus |
E2 | - |
Homo sapiens |
E2 | - |
Rattus norvegicus |
More | the enzyme is a subunit of the pyruvate dehydrogenase multienzyme complex, 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 |
More | the enzyme is a subunit of the pyruvate dehydrogenase multienzyme complex, 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 | Rattus norvegicus |