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Literature summary extracted from

  • Korotchkina, L.G.; Patel, M.S.
    Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase (2001), J. Biol. Chem., 276, 37223-37229.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.2 dihydrolipoyl transacetylase degree of interaction and mechanism differ for the 4 different isozymes Rattus norvegicus
2.7.11.2 dihydrolipoyl transacetylase degree of interaction and mechanism differ for the 4 different isozymes Mammalia
2.7.11.2 dihydrolipoyl transacetylase degree of interaction and mechanism differ for the 4 different isozymes Homo sapiens
2.7.11.2 dihydrolipoyl transacetylase activation in presence of a binding protein, referred to as dihydrolipoamide dehydrogenase-binding protein Rattus norvegicus
2.7.11.2 dihydrolipoyl transacetylase activation in presence of a binding protein, referred to as dihydrolipoamide dehydrogenase-binding protein Homo sapiens
2.7.11.2 dihydrolipoyl transacetylase activation depends on the buffer system, the isozyme and the reduction status of the lipoyl groups Rattus norvegicus
2.7.11.2 dihydrolipoyl transacetylase activation depends on the buffer system, the isozyme and the reduction status of the lipoyl groups Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.2 overexpression of isozyme PDK3 in Escherichia coli BL21(DE3) as His-tagged protein Homo sapiens
2.7.11.2 overexpression of isozymes PDK1, PDK2, and PDK4 in Escherichia coli BL21(DE3) as His-tagged proteins Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.2 Mg2+
-
 Homo sapiens
2.7.11.2 Mg2+
-
 Mammalia
2.7.11.2 Mg2+
-
 Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] Mammalia catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 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
2.7.11.2 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

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.2 Homo sapiens
-
 isozyme PDK3
-
2.7.11.2 Mammalia
-
 at least 4 different isozymes: PDK1, PDK2, PDK3, PDK4
-
2.7.11.2 Rattus norvegicus
-
 3 isozymes PDHK1, PDHK2, PDHK4
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.2 additional information tissue-specific expression, regulation mechanisms Rattus norvegicus
-
2.7.11.2 additional information tissue-specific expression, regulation mechanisms Mammalia
-
2.7.11.2 additional information tissue-specific expression, regulation mechanisms Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.11.2 additional information
-
 activity depends on the buffer system, the reduction status of the lipoyl groups and on the serine phosphorylation site of the E1 subunit of the pyruvate dehydrogenase complex used as substrate Rattus norvegicus
2.7.11.2 additional information
-
 activity depends on the buffer system, the reduction status of the lipoyl groups and on the serine phosphorylation site of the E1 subunit of the pyruvate dehydrogenase complex used as substrate Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.2 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
2.7.11.2 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
2.7.11.2 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
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] the 3 serine phosphorylation sites of the E1 subunit are specifically and with different activity phosphorylated by the 4 isozymes, overview: site 1 is preferably utilized by PDK2, site 2 by PDK3, and site 3 is exclusively utilized by PDK1 Homo sapiens ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] the 3 serine phosphorylation sites of the E1 subunit are specifically and with different activity phosphorylated by the 4 isozymes, overview: site 1 is preferably utilized by PDK2, site 2 by PDK3, and site 3 is exclusively utilized by PDK1 Rattus norvegicus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Mammalia ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 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
2.7.11.2 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
2.7.11.2 additional information activity depends on the buffer system, the reduction status of the lipoyl groups and on the serine phosphorylation site of the E1 subunit of the pyruvate dehydrogenase complex used as substrate Homo sapiens ?
-
 ?
2.7.11.2 additional information activity depends on the buffer system, the reduction status of the lipoyl groups and on the serine phosphorylation site of the E1 subunit of the pyruvate dehydrogenase complex used as substrate Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.2 PDK
-
 Rattus norvegicus
2.7.11.2 PDK
-
 Mammalia
2.7.11.2 PDK
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.2 30
-
 assay at Homo sapiens
2.7.11.2 30
-
 assay at Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.11.2 0.0383
-
 [Pyruvate dehydrogenase (lipoamide)] phosphorylation site 3 of subunit E1, isozyme PDK1, pH 7.0, 30°C Rattus norvegicus
2.7.11.2 0.0933
-
 [Pyruvate dehydrogenase (lipoamide)] phosphorylation site 2 of subunit E1, isozyme PDK3, pH 7.0, 30°C Rattus norvegicus
2.7.11.2 0.108
-
 [Pyruvate dehydrogenase (lipoamide)] phosphorylation site 2 of subunit E1, isozyme PDK4, pH 7.0, 30°C Rattus norvegicus
2.7.11.2 0.11
-
 [Pyruvate dehydrogenase (lipoamide)] phosphorylation site 1 of subunit E1, isozyme PDK1, pH 7.0, 30°C Rattus norvegicus
2.7.11.2 0.277
-
 [Pyruvate dehydrogenase (lipoamide)] phosphorylation site 1 of subunit E1, isozyme PDK2, pH 7.0, 30°C Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.2 additional information
-
 different buffer systems Rattus norvegicus
2.7.11.2 additional information
-
 different buffer systems Homo sapiens

Cofactor

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