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Literature summary extracted from

  • Korotchkina, L.G.; Patel, M.S.
    Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex (2008), FEBS Lett., 582, 468-472.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.4.1 expressed in Escherichia coli BL21 cells Homo sapiens
2.3.1.12 a recombinant fragment hL2S (containing the second lipoyl domain (L2), second hinge region, E1-binding domain (S) and third hinge region of hE2, residues 128–330) is overexpressed in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.2.4.1 D289A the beta subunit mutant does not have any detectable activity in assays with NAD+ and shows no change in activity in 2,6-dichlorophenolindophenol assays Homo sapiens
1.2.4.1 D289N the beta subunit mutant shows by 36% reduced activity in assays with NAD+ Homo sapiens
1.2.4.1 E229A the beta subunit mutant does not show drastic changes compared to the wild type E1 activities Homo sapiens
1.2.4.1 E229Q the beta subunit mutant does not show drastic changes compared to the wild type E1 activities Homo sapiens
1.2.4.1 E232A the beta subunit mutant does not show drastic changes compared to the wild type E1 activities Homo sapiens
1.2.4.1 E232Q the beta subunit mutant does not show drastic changes compared to the wild type E1 activities Homo sapiens
1.2.4.1 E234A the beta subunit mutant does not show drastic changes compared to the wild type E1 activities Homo sapiens
1.2.4.1 E234Q the beta subunit mutant does not show drastic changes compared to the wild type E1 activities Homo sapiens
1.2.4.1 I329A shows 37-43% reduction in activity compared to the wild type enzyme Homo sapiens
1.2.4.1 additional information mutant I329DELTA (deletion at the C-terminal of E1) shows 62% reduction in activity compared to the wild type enzyme Homo sapiens
2.3.1.12 K276A mutant shows negligible binding to human pyruvate dehydrogenase with 86fold higher KD compared to wild-type Homo sapiens
2.3.1.12 R297A mutant is found to have KD 6.8fold higher than that for the wild-type, indicating a possible involvement of this residue in the interaction with human pyruvate dehydrogenase, but not with the C-terminal residue of beta-subunit Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.12 additional information Homo sapiens in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2) ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.1 Homo sapiens
-
-
-
2.3.1.12 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.4.1 Ni-NTA column chromatography Homo sapiens
2.3.1.12 using Ni-nitrilotriacetate-agarose affinity chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.4.1 pyruvate + CoA + NAD+
-
 Homo sapiens acetyl-CoA + CO2 + NADH
-
 ?
1.2.4.1 pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
-
 Homo sapiens acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
 ?
2.3.1.12 additional information in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2) Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.4.1 heterotetramer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.2.4.1 pyruvate dehydrogenase E1 bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2) in pyruvate dehydrogenase complex (PDC) Homo sapiens
2.3.1.12 dihydrolipoyl acetyltransferase
-
 Homo sapiens
2.3.1.12 hE2
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.1 NAD+
-
 Homo sapiens
1.2.4.1 thiamine diphosphate
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.3.1.12 physiological function in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). K276 of hE2 is involved in the interaction with pyruvate dehydrogenase Homo sapiens