Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.12 extracted from

  • Roche, T.E.; Hiromasa, Y.; Turkan, A.; Gong, X.; Peng, T.; Yan, X.; Kasten, S.A.; Bao, H.; Dong, J.
    Central organization of mammalian pyruvate dehydrogenase (PD) complex and lipoyl domain-mediated activated function and control of PD kinases and phosphatase 1 (2004), Oxid. Stress Dis., 11, 363-386.
No PubMed abstract available
Search for more literature for 2.3.1.12

Protein Variants

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

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 [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

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 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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

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

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

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