Literature summary extracted from

Rochet, J.C.; Brownie, E.R.; Oikawa, K.; Hicks, L.D.; Fraser, M.E.; James, M.N.; Kay, C.M.; Bridger, W.A.; Wolodko, W.T.
Pig heart CoA transferase exists as two oligomeric forms separated by a large kinetic barrier (2000), Biochemistry, 39, 11291-11302.

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.8.3.5	additional information	mutant with deletion of amino acid residues 249-254 shows no altered kinetic values	Sus scrofa

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
2.8.3.5	101000	-	dimeric form, sedimentation equilibrium experiments	Sus scrofa
2.8.3.5	218000	-	tetrameric form, sedimentation equilibrium experiments	Sus scrofa

Organism

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

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.8.3.5	succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA	mechanism	Sus scrofa	a

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	enzyme exists as a tetramer and as a dimer, dissociation of the tetramer to the dimer occurs in benign solutions containing high salt concentrations. Full convertion to the homodimeric form occurs during refolding from denaturant at low protein concentrations	Sus scrofa
2.8.3.5	tetramer	enzyme exists as a tetramer and as a dimer, dissociation of the tetramer to the dimer occurs in benign solutions containing high salt concentrations. Full convertion to the homodimeric form occurs during refolding from denaturant at low protein concentrations	Sus scrofa

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Release 2023.1 (January 2023)