Literature summary for 6.2.1.5 extracted from

Khan, I.A.; Nishimura, J.S.
Native-like intermediate on the folding pathway of Escherichia coli succinyl-CoA synthetase (1988), J. Biol. Chem., 263, 2152-2158.

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
enzyme that is completely inactivated by 0.6 M guanidine hydrochloride, but contains 90% residual native structure, can refold back to fully active enzyme. Enzyme denatured in 1.5 M and 6.0 M guanidine hydrochloride, that is catalytically inactive and devoid of a large fraction of the native enzyme structure, can also regain the native structure upon refolding, but the refolded structures are only 86% and 71% active, respectively	Escherichia coli

Renatured (Comment)

Organism

enzyme that is completely inactivated by 0.6 M guanidine hydrochloride, but contains 90% residual native structure, can refold back to fully active enzyme. Enzyme denatured in 1.5 M and 6.0 M guanidine hydrochloride, that is catalytically inactive and devoid of a large fraction of the native enzyme structure, can also regain the native structure upon refolding, but the refolded structures are only 86% and 71% active, respectively

Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + succinate + CoA	-	Escherichia coli	ADP + phosphate + succinyl-CoA	-	?

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Release 2023.1 (January 2023)