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Literature summary extracted from

  • Tanaka, N.; Koike, K.; Otsuka, K.I.; Hamada, M.; Ogasahara, K.; Koike, M.
    Mammalian alpha-keto acid dehydrogenase complexes. 8. Properties and subunit composition of the pig heart lipoate succinyltransferase (1974), J. Biol. Chem., 249, 191-198.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.3.1.61 lyophilized enzyme loses more than 50% of its original activity Sus scrofa
2.3.1.61 stable to frequent freezing and thawing Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.61 41000
-
 24 * 41000, sedimentation equilibrium Sus scrofa
2.3.1.61 48000
-
 24 * 48000, SDS-PAGE Sus scrofa
2.3.1.61 958000
-
 analytical ultracentrifugation Sus scrofa
2.3.1.61 992000 1027000 different preparations of the enzyme, analytical ultracentrifugation Sus scrofa
2.3.1.61 1000000
-
 sedimentation equlibrium Sus scrofa

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 + dihydrolipoamide Sus scrofa plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex CoA + S-succinyldihydrolipoamide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.61 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.61
-
 Sus scrofa

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.3.1.61 10% recovery of enzyme activity after renaturation of SDS denatured enzyme (3%) Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.61 heart
-
 Sus scrofa
-
2.3.1.61 muscle
-
 Sus scrofa
-

Storage Stability

EC Number Storage Stability Organism
2.3.1.61 -18°C, 0.05 M potassium phosphate buffer, pH 7.0, containing 0.05 mM EDTA, stable for over 6 months without significant loss of activity, despite frequent freezing and thawing Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.61 succinyl-CoA + dihydrolipoamide
-
 Sus scrofa CoA + S-succinyldihydrolipoamide
-
 ?
2.3.1.61 succinyl-CoA + dihydrolipoamide plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex Sus scrofa CoA + S-succinyldihydrolipoamide
-
 ?
2.3.1.61 succinyl-CoA + dihydrolipoic acid
-
 Sus scrofa CoA + succinyldihydrolipoate
-
 ?
2.3.1.61 succinyl-CoA + dihydrolipoyllysine
-
 Sus scrofa CoA + succinyldihydrolipoyllysine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.61 polymer 24 * 48000, SDS-PAGE Sus scrofa
2.3.1.61 polymer 24 * 41000, sedimentation equilibrium Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.61 30
-
 at pH 7.2 Sus scrofa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.61 70
-
 loss of activity is slow up to 70°C, but rapid beyond 75°C Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.61 7.2
-
-
 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.61 Lipoyl-protein enzyme contains 8 mol of protein-bound lipoic acid per mol of enzyme Sus scrofa