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Literature summary extracted from

  • Fraser, M.E.; Joyce, M.A.; Ryan, D.G.; Wolodko, W.T.
    Two glutamate residues,Glu 208alpha and Glu 197beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase (2002), Biochemistry, 41, 537-546.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.2.1.5 wild-type and mutant enzyme E197betaA, hanging drop vapour diffusion method Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.5 E197betaA mutant enzyme with very low activity. The mutant protein is crystallized in the same space group as the wild-type enzyme. Crystals of the mutant enzyme grew as plates rather than as cubes which are the usual crystal habit for the wild-type enzyme Escherichia coli
6.2.1.5 E197betaD the Km-values and turnover numbers are comparable to those of the wild-type enzyme Escherichia coli
6.2.1.5 E197betaQ the KM-value for each substrate is comparable to that of the wild-type enzyme, except for GTP, whose Km-value is reduced by a factor of 20. 3000fold decrease in turnover number for reaction with ATP, 7000fold decrease in turnover-number when using GTP Escherichia coli
6.2.1.5 E208alphaD Km-values for succinate, CoA, GTP and ATP are comparable to those observed with wild-type enzyme. The turnover-numbers for ATP and GTP are comparable to the wild-type value Escherichia coli
6.2.1.5 E208alphaQ Km-values for succinate, CoA and ATP are comparable to those observed with wild-type enzyme. The KM-value for GTP is 36times lower than that of the wild-type enzyme. The turnover-numbers for ATP and GTP are reduced approximately 5000fold compared to the wild-type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.5 0.0013
-
 CoA pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 0.0018
-
 CoA pH 7.4, 22°C, mutant enzyme E197betaQ Escherichia coli
6.2.1.5 0.002
-
 CoA pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli
6.2.1.5 0.0027
-
 CoA pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 0.011
-
 GTP pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 0.02
-
 GTP pH 7.4, 22°C, mutant enzyme E197betaQ Escherichia coli
6.2.1.5 0.041
-
 ATP pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 0.063
-
 GTP pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli
6.2.1.5 0.106
-
 ATP pH 7.4, 22°C, mutant enzyme E197betaQ Escherichia coli
6.2.1.5 0.116
-
 ATP pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli
6.2.1.5 0.137
-
 ATP pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 0.26
-
 succinate pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli
6.2.1.5 0.27
-
 succinate pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 0.311
-
 GTP pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 0.4
-
 succinate pH 7.4, 22°C, mutant enzyme E197betaQ Escherichia coli
6.2.1.5 0.87
-
 succinate pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
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 ATP + succinate + CoA during the reaction a His residue at the alpha-subunit is transiently phosphorylated. Glu208alpha and Glu197beta, are crucial for phosphorylation and dephosphorylation of the active-site His Escherichia coli ADP + phosphate + succinyl-CoA
-
 ?
6.2.1.5 GTP + succinate + CoA
-
 Escherichia coli GDP + phosphate + succinyl-CoA
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2.1.5 0.21
-
 GTP pH 7.4, 22°C, mutant enzyme E197betaQ Escherichia coli
6.2.1.5 0.28
-
 GTP pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 0.57
-
 ATP pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 0.85
-
 ATP pH 7.4, 22°C, mutant enzyme E197betaQ Escherichia coli
6.2.1.5 6.08
-
 ATP pH 7.4, 22°C, mutant enzyme E208alphaQ Escherichia coli
6.2.1.5 302
-
 GTP pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli
6.2.1.5 1775
-
 ATP pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 1775
-
 GTP pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 1780
-
 ATP pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 1780
-
 GTP pH 7.4, 22°C, mutant enzyme E197betaD Escherichia coli
6.2.1.5 2340
-
 ATP pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli
6.2.1.5 2343
-
 ATP pH 7.4, 22°C, mutant enzyme E208alphaD Escherichia coli