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Literature summary for 2.7.11.2 extracted from

  • Roche, T.E.; Hiromasa, Y.; Turkan, A.; Gong, X.; Peng, T.; Yan, X.; Kasten, S.A.; Bao, H.; Dong, J.
    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.
    View publication on PubMed
Search for more literature for 2.7.11.2

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA
-
 Rattus norvegicus
acetyl-CoA activates the enzyme, especially isozyme PDK2 Mammalia
acetyl-CoA domain-specific binding, isozymes PDK2 and PDK3 Mammalia
acetyl-CoA domain-specific binding, isozymes PDK2 and PDK3 Homo sapiens
dihydrolipoyl transacetylase domaine-specific binding, isozymes PDK2 and PDK3, the latter binding more tightly to the L2 domain Mammalia
dihydrolipoyl transacetylase degree of interaction and mechanism differ for the 4 different isozymes Mammalia
dihydrolipoyl transacetylase degree of interaction and mechanism differ for the 4 different isozymes Homo sapiens
dihydrolipoyl transacetylase degree of interaction and mechanism differ for the 4 different isozymes Rattus norvegicus
dihydrolipoyl transacetylase isozyme PDK2 can phosphorylate free pyruvate dehydrogenase complex but bound dihydrolipoyl transacetylase enhances the rate up to 5000fold Mammalia
dihydrolipoyl transacetylase binding and activation mechanism Mammalia
dihydrolipoyl transacetylase dynamic, effector-modified interactions of the regulatory isozymes with the flexibly held outer domains of the core-forming dihydrolipoyl acetyl transferase component of pyruvate dehydrogenase complex to adapt the complex activity, regulatory mechanism Mammalia
dihydrolipoyl transacetylase dynamic, effector-modified interactions of the regulatory isozymes with the flexibly held outer domains of the core-forming dihydrolipoyl acetyl transferase component of pyruvate dehydrogenase complex to adapt the complex activity, regulatory mechanism Homo sapiens
dihydrolipoyl transacetylase dynamic, effector-modified interactions of the regulatory isozymes with the flexibly held outer domains of the core-forming dihydrolipoyl acetyl transferase component of pyruvate dehydrogenase complex to adapt the complex activity, regulatory mechanism Rattus norvegicus
fatty acids leads to overexpression of isozyme PDK4 via mechanism involving peroxisome proliferator-activated receptor-alpha Mammalia
glucocorticoids leads to overexpression of isozyme PDK4 via mechanism involving peroxisome proliferator-activated receptor-alpha Mammalia
additional information starvation increases expression of isozyme PDK4 Mammalia
additional information starvation increases expression of isozyme PDK4 Rattus norvegicus
NADH
-
 Rattus norvegicus
NADH activates the enzyme, especially isozyme PDK2 Mammalia
NADH domain-specific binding, isozymes PDK2 and PDK3 Mammalia
NADH domain-specific binding, isozymes PDK2 and PDK3 Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of isozyme PDK4 in Escherichia coli, unmodified and modified enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ADP synergism with pyruvate Homo sapiens
ADP isozyme PDK2: synergistic with phosphate; synergism with pyruvate Mammalia
ADP synergism with pyruvate Rattus norvegicus
Insulin blockage of the expression of isozyme PDK4 via insulin-activated pathway Mammalia
additional information
-
 Homo sapiens
additional information isozyme PDK3 undergoes self-association in absence of dihydrolipoyl transacetylase domain L2 leading to a decrease in activity; starvation and diabetes reduce the expression of isozyme PDK2 Mammalia
phosphate isozyme PDK2, synergistically with ADP and pyruvate Mammalia
pyruvate very weak inhibition Homo sapiens
pyruvate isozyme PDK2: synergistic with phosphate; isozyme PDK3; very weak inhibition Mammalia
pyruvate very weak inhibition Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Mammalia 5739
-
mitochondrion
-
 Homo sapiens 5739
-
mitochondrion
-
 Rattus norvegicus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [pyruvate dehydrogenase (lipoamide)] Mammalia the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Homo sapiens the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Rattus norvegicus the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Mammalia tissue-specific regulation of the pyruvate dehydrogenase complex in order to adjust glucose consumption ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Homo sapiens tissue-specific regulation of the pyruvate dehydrogenase complex in order to adjust glucose consumption ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Rattus norvegicus tissue-specific regulation of the pyruvate dehydrogenase complex in order to adjust glucose consumption ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Mammalia catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Homo sapiens catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Rattus norvegicus catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] Rattus norvegicus high-fat feeding increases the expression of isozyme PDK2, but not of PDK4, hyperthyroidism increases the expression of both isozymes, physiological implications ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 4 different isozymes: PDK1, PDK2, PDK3, PDK4
-
Mammalia
-
 at least 4 different isozymes: PDK1, PDK2, PDK3, PDK4
-
Rattus norvegicus
-
 4 different isozymes: PDK1, PDK2, PDK3, PDK4
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Mammalia
-
heart
-
 Rattus norvegicus
-
kidney
-
 Mammalia
-
kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [pyruvate dehydrogenase (lipoamide)] pyruvate dehydrogenase complex substrate is inactivated by ATP-dependent phosphorylation of 3 serine residues on the E1 subunit Mammalia ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] pyruvate dehydrogenase complex substrate is inactivated by ATP-dependent phosphorylation of 3 serine residues on the E1 subunit Homo sapiens ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] pyruvate dehydrogenase complex substrate is inactivated by ATP-dependent phosphorylation of 3 serine residues on the E1 subunit Rattus norvegicus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] isozyme PDK2 can phosphorylate free pyruvate dehydrogenase complex but bound dihydrolipoyl transacetylase enhances the rate up to 5000fold Mammalia ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex Mammalia ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex Homo sapiens ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex Rattus norvegicus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] tissue-specific regulation of the pyruvate dehydrogenase complex in order to adjust glucose consumption Mammalia ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] tissue-specific regulation of the pyruvate dehydrogenase complex in order to adjust glucose consumption Homo sapiens ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] tissue-specific regulation of the pyruvate dehydrogenase complex in order to adjust glucose consumption Rattus norvegicus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Mammalia ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Homo sapiens ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Rattus norvegicus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
ATP + [pyruvate dehydrogenase (lipoamide)] high-fat feeding increases the expression of isozyme PDK2, but not of PDK4, hyperthyroidism increases the expression of both isozymes, physiological implications Rattus norvegicus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir

Synonyms

Synonyms Comment Organism
PDK
-
 Mammalia
PDK
-
 Homo sapiens
PDK
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Mammalia
ATP dependent on Homo sapiens
ATP dependent on Rattus norvegicus