Literature summary for 6.2.1.4 extracted from

Nishimura, J.S.; Ybarra J.; Mitchell, T.; Horowitz P.M.
Isolation, amino acid analysis and refolding of subunits of pig heart succinyl-CoA synthetase (1988), Biochem. J., 250, 429-434.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.014	-	GTP	refolded enzyme	Sus scrofa
0.027	-	GTP	native enzyme	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
refolded from its isolated subunit after denaturation. Refolding of enzyme denatured in 6 M guanidine hydrochloride or of alpha- and beta-subunits isolated in the solvent requires the presence of either ethylene glycol or glycerol, optimally at 20-25% (v/v). MgGTP2- does not stimulate reactivation of the enzyme. Yields of 60% and 40% are obtained in the refolding of denatured enzyme and isolated subunits respectively	Sus scrofa

Renatured (Comment)

Organism

refolded from its isolated subunit after denaturation. Refolding of enzyme denatured in 6 M guanidine hydrochloride or of alpha- and beta-subunits isolated in the solvent requires the presence of either ethylene glycol or glycerol, optimally at 20-25% (v/v). MgGTP2- does not stimulate reactivation of the enzyme. Yields of 60% and 40% are obtained in the refolding of denatured enzyme and isolated subunits respectively

Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + succinate + CoA	-	Sus scrofa	GDP + phosphate + succinyl-CoA	-	?

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Release 2023.1 (January 2023)