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Literature summary extracted from

  • Chakraborty, J.; Nemeria, N.S.; Farinas, E.; Jordan, F.
    Catalysis of transthiolacylation in the active centers of dihydrolipoamide acyltransacetylase components of 2-oxo acid dehydrogenase complexes (2018), FEBS Open Bio, 8, 880-896 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.61 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.61 D374A the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 2.1% compared to the wild type enzyme Escherichia coli
2.3.1.61 D374N the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.7% compared to the wild type enzyme Escherichia coli
2.3.1.61 D379A the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.5% compared to the wild type enzyme Escherichia coli
2.3.1.61 H375A the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 2fold compared to the wild type enzyme Escherichia coli
2.3.1.61 H375C the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 1% compared to the wild type enzyme Escherichia coli
2.3.1.61 H375G the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 5fold compared to the wild type enzyme Escherichia coli
2.3.1.61 H375N the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 0.5% compared to the wild type enzyme Escherichia coli
2.3.1.61 H375W the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 54fold compared to the wild type enzyme Escherichia coli
2.3.1.61 R376A the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 56% compared to the wild type enzyme Escherichia coli
2.3.1.61 T323A the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 45% compared to the wild type enzyme Escherichia coli
2.3.1.61 T323S the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 43% compared to the wild type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.61 succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine Escherichia coli
-
 CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.61 Escherichia coli P0AFG6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.61 Ni-Sepharose 6 column chromatography and Sephacryl S-300 gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.61 succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
-
 Escherichia coli CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
 r

Subunits

EC Number Subunits Comment Organism
2.3.1.61 ? x * 11420, lipoyl domain, calculated from amino acid sequence Escherichia coli
2.3.1.61 ? x * 11421, lipoyl domain, mass spectrometry Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.61 dihydrolipoamide acyltransacetylase
-
 Escherichia coli
2.3.1.61 E2o component of the 2-oxoglutarate dehydrogenase complex Escherichia coli