Literature summary for 6.2.1.5 extracted from

Bailey, D.L.; Fraser, M.E.; Bridger, W.A.; James, M.N.; Wolodko, W.T.
A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis (1999), J. Mol. Biol., 285, 1655-1666.

Protein Variants

Protein Variants	Comment	Organism
E231betaA	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
E231betaW	strong decrease in activity	Escherichia coli
E231betaW/Q247betaW/E249betaW	strong decrease in activity	Escherichia coli
E29betaD/E33betaA/S36betaA	activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact	Escherichia coli
E33betaA/S36betaA	activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact	Escherichia coli
E33betaA/S36betaA/K66betaA	activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact	Escherichia coli
E4betaK/R14betaD//R70betaG/E231betaW/Q247betaW/E24	strong decrease in activity	Escherichia coli
E74betaK	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
K66betaA	activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact	Escherichia coli
M156betaD/Y1258betaD/R161betaE/E162betaR	mutant enzyme with alphabeta-dimer subunit structure	Escherichia coli
Q247betaK	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R14betaD	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R14betaD/E231betA	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R14betaD/R70betaG/E74betaK	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R14betaD/R70betaG/E74betaK/E231betaA/Q247betaK	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R29betaA/E33betaA/S36betaA/K66betaA	strong decrease in activity	Escherichia coli
R29betaD	activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact	Escherichia coli
R70betaG	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R70betaG/E74betaK	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli
R70betaG/E74betaK/Q247betaK	activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP + phosphate + succinyl-CoA	Escherichia coli	the enzyme carries out the substrate-level phosphorylation in the citric acid cycle	ATP + succinate + CoA	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + phosphate + succinyl-CoA	the enzyme carries out the substrate-level phosphorylation in the citric acid cycle	Escherichia coli	ATP + succinate + CoA	-	?

Subunits

Subunits	Comment	Organism
tetramer	2 * alpha + 2 * beta. The dimerization of the alphabeta-dimer is not a prerequisite for catalytic competency nor for alternating sites cooperativity in the tetramer	Escherichia coli