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Literature summary 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.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.5 E231betaA activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure Escherichia coli
6.2.1.5 E231betaW strong decrease in activity Escherichia coli
6.2.1.5 E231betaW/Q247betaW/E249betaW strong decrease in activity Escherichia coli
6.2.1.5 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
6.2.1.5 E33betaA/S36betaA activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact Escherichia coli
6.2.1.5 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
6.2.1.5 E4betaK/R14betaD//R70betaG/E231betaW/Q247betaW/E24 strong decrease in activity Escherichia coli
6.2.1.5 E74betaK activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure Escherichia coli
6.2.1.5 K66betaA activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact Escherichia coli
6.2.1.5 M156betaD/Y1258betaD/R161betaE/E162betaR mutant enzyme with alphabeta-dimer subunit structure Escherichia coli
6.2.1.5 Q247betaK activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure Escherichia coli
6.2.1.5 R14betaD activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure Escherichia coli
6.2.1.5 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
6.2.1.5 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
6.2.1.5 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
6.2.1.5 R29betaA/E33betaA/S36betaA/K66betaA strong decrease in activity Escherichia coli
6.2.1.5 R29betaD activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact Escherichia coli
6.2.1.5 R70betaG activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure Escherichia coli
6.2.1.5 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
6.2.1.5 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)

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

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.5 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.5
-
 Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
6.2.1.5 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