Literature summary for 2.8.3.5 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.

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Protein Variants

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Reaction

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

Subunits

Subunits	Comment	Organism
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
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)