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Literature summary for 2.7.11.2 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

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

Cloned(Commentary)

Cloned (Comment) Organism
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
functional expression in Escherichia coli as His-tagged protein Caenorhabditis elegans
functional expression in Escherichia coli strain BL21(DE3) as His-tagged protein Ascaris suum

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
Trypsin
-
Ascaris suum
Trypsin
-
Caenorhabditis elegans

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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

Organism UniProt Comment Textmining
Ascaris suum O02623
-
-
Caenorhabditis elegans
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Ascaris suum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.74
-
purified recombinant enzyme, in presence of NADH and acetyl-CoA Caenorhabditis elegans
0.92
-
purified recombinant enzyme, in presence of NADH and acetyl-CoA Ascaris suum

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Caenorhabditis elegans
ATP dependent on Ascaris suum