Literature summary for 2.8.3.5 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.

Search for more literature for 2.8.3.5

Cloned(Commentary)

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
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)

Renatured (Comment)	Organism
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

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

Subunits

Subunits	Comment	Organism
dimer	-	Sus scrofa

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Release 2023.1 (January 2023)