Literature summary for 6.2.1.5 extracted from

Luo, G.X.; Nishimura, J.S.
Adenosine 5�-tetraphosphate is synthesized by the histidine alpha142-->asparagine mutant of Escherichia coli succinyl-CoA synthetase (1992), J. Biol. Chem., 267, 9516-9520.

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Protein Variants

Protein Variants	Comment	Organism
N142N	mutant H142N is devoid of the ability to catalyze the overall reaction but is able to catalyze the half-reactions at significant rates. Phosphorylation by ATP and dephosphorylation by ADP of the mutant enzyme occurs at rates that are at least 10times greater than those with wild type enzyme. Dephosphorylation by succinate plus CoA, succinyl-CoA formation, proceeds with a maximal velocity of 10% that of wild type enzyme	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
ADP	adenosine 5´-tetraphosphate formation	Escherichia coli
CoA plus succinate	presence of succinate plus CoA inhibits adenosine 5'-tetraphosphate formation	Escherichia coli
succinate	presence of succinate plus CoA inhibits adenosine 5'-tetraphosphate formation	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0145	-	ATP	adenosine 5´-tetraphosphate formation	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	wild type and mutant H142N	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + ATP	-	Escherichia coli	adenosine 5'-tetraphosphate + ADP	-	?
ATP + succinate + CoA	-	Escherichia coli	ADP + phosphate + succinyl-CoA	-	?
beta,gamma-methylene-adenosine 5'-triphosphate	-	Escherichia coli	beta,gamma-methylene-adenosine 5'-tetraphosphate + ?	alpha,gamma-methylene adenosine tetraphosphate	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

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Release 2023.1 (January 2023)