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Literature summary extracted from

  • Chen, W.; Komuniecki, P.R.; Komuniecki, R.
    Nematode pyruvate dehydrogenase kinases: role of the C-terminus in binding to the dihydrolipoyl transacetylase core of the pyruvate dehydrogenase complex (1999), Biochem. J., 339, 103-109.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.2 acetyl-CoA kinase bound to transacetylase core Caenorhabditis elegans
2.7.11.2 acetyl-CoA kinase bound to transacetylase core Ascaris suum
2.7.11.2 acetyl-CoA synergism with NADH Caenorhabditis elegans
2.7.11.2 acetyl-CoA synergism with NADH Ascaris suum
2.7.11.2 dihydrolipoyl transacetylase pyruvate dehydrogenase-complex transacetylase core Caenorhabditis elegans
2.7.11.2 dihydrolipoyl transacetylase pyruvate dehydrogenase-complex transacetylase core Ascaris suum
2.7.11.2 NADH kinase bound to transacetylase core Caenorhabditis elegans
2.7.11.2 NADH kinase bound to transacetylase core Ascaris suum
2.7.11.2 NADH synergism with acetyl-CoA Caenorhabditis elegans
2.7.11.2 NADH synergism with acetyl-CoA Ascaris suum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.2 expression of truncated enzyme forms, comprising residues 284-402 and 1-334, respectively, as maltose-binding-protein fusion proteins in Escherichia coli JM109 Caenorhabditis elegans
2.7.11.2 functional expression in Escherichia coli as His-tagged protein Caenorhabditis elegans
2.7.11.2 functional expression in Escherichia coli strain BL21(DE3) as His-tagged protein Ascaris suum

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.2 additional information construction of truncated enzyme forms, the N-terminally truncated form, residues 284-402, is catalytically inactive, the C-terminally reduced form, residues 1-334, shows reduced activity Caenorhabditis elegans

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.2 Trypsin
-
 Ascaris suum
2.7.11.2 Trypsin
-
 Caenorhabditis elegans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.2 Mg2+
-
 Caenorhabditis elegans
2.7.11.2 Mg2+
-
 Ascaris suum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.11.2 45000
-
 2 * 45000, recombinant wild-type, SDS-PAGE Caenorhabditis elegans
2.7.11.2 76000
-
 recombinant wild-type, gel filtration Caenorhabditis elegans

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)] Caenorhabditis elegans 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)] Ascaris suum 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 Ascaris suum O02623
-
-
2.7.11.2 Caenorhabditis elegans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.2 recombinant from Escherichia coli as His-tagged protein to homogeneity Ascaris suum
2.7.11.2 recombinant wild-type and truncated form from Escherichia coli as His-tagged and maltose-binding fusion protein, respectively, to homogeneity Caenorhabditis elegans

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.2 muscle
-
 Ascaris suum
-

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 0.74
-
 purified recombinant enzyme, in presence of NADH and acetyl-CoA Caenorhabditis elegans
2.7.11.2 0.92
-
 purified recombinant enzyme, in presence of NADH and acetyl-CoA Ascaris suum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)]
-
 Caenorhabditis elegans ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)]
-
 Ascaris suum 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 Caenorhabditis elegans 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 Ascaris suum ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 additional information no autophosphorylation Caenorhabditis elegans ?
-
 ?
2.7.11.2 additional information no autophosphorylation Ascaris suum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.11.2 dimer
-
 Ascaris suum
2.7.11.2 dimer 2 * 45000, recombinant wild-type, SDS-PAGE Caenorhabditis elegans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.2 37
-
 assay at Caenorhabditis elegans
2.7.11.2 37
-
 assay at Ascaris suum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.2 7.4
-
 assay at Caenorhabditis elegans
2.7.11.2 7.4
-
 assay at Ascaris suum

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.2 ATP dependent on Caenorhabditis elegans
2.7.11.2 ATP dependent on Ascaris suum