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Literature summary extracted from

  • Rochet, J.C.; Oikawa, K.; Hicks, L.D.; Kay, C.M.; Bridger, W.A.; Wolodko, W.T.
    Productive interactions between the two domains of pig heart CoA transferase during folding and assembly (1997), Biochemistry, 36, 8807-8820.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.5 N-terminal and C-terminal domain Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.3.5 52000
-
 SDS-PAGE Sus scrofa
2.8.3.5 53200
-
 C-terminal domain, sedimentation equilibrium experiments Sus scrofa
2.8.3.5 53200
-
 N-terminal domain, sedimentation equilibrium experiments Sus scrofa
2.8.3.5 915000
-
 sedimentation equilibrium experiments Sus scrofa

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.5 N-terminal and C-terminal domain, a mixture of the domains is only active when domains are isolated in the presence of 2-mercaptoethanol Sus scrofa

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.8.3.5 intact hydrophilic peptide which links the 2 domains is essential for the recovery of activity observed upon refolding of the denatured enzyme in vitro Sus scrofa

Source Tissue

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

Subunits

EC Number Subunits Comment Organism
2.8.3.5 dimer
-
 Sus scrofa