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Literature summary extracted from

  • Fraser, M.E.; Hayakawa, K.; Brown, W.D.
    Catalytic role of the conformational change in succinyl-CoA:3-oxoacid CoA transferase on binding CoA (2010), Biochemistry, 49, 10319-10328.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.5 expressed in Escherichia coli BL21(DE3) cells Sus scrofa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.3.5 hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 100 mM Tris-HCl (pH8.5) Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.3.5 succinyl-CoA + acetoacetate Sus scrofa
-
 succinate + acetoacetyl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.5 Sus scrofa Q29551
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.5 Ni-NTA agarose column chromatography and Ultrogel AcA 44 column chromatography Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.3.5 heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.5 succinyl-CoA + acetoacetate
-
 Sus scrofa succinate + acetoacetyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.3.5 dimer x-ray crystallography Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
2.8.3.5 SCOT
-
 Sus scrofa
2.8.3.5 succinyl-CoA:3-oxoacid CoA transferase
-
 Sus scrofa