EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.2.1.4 | purified enzyme in complex with GDP-Mn2+, protein in 50 mM KCl, 0.1 mM EDTA, 50 mM Tris-HCl, pH 7.4, X-ray diffraction structure determination and analysis at 2.35 A resolution | Thermus aquaticus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.4 | guanidinium hydrochloride | inactivation at 0.5 M | Thermus aquaticus | |
6.2.1.4 | Urea | the Thermus aquaticus enzyme loses activity at 4-5.5 M urea, but it regains activity with increasing concentrations of urea, reaching 70% of its original activity in 8.5 M urea | Thermus aquaticus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.4 | Mg2+ | required for catalysis, Mn2+ can replace Mg2+ in catalysis | Thermus aquaticus | |
6.2.1.4 | Mn2+ | Mn2+ can replace Mg2+ in catalysis | Thermus aquaticus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.4 | ATP + succinate + CoA | Thermus aquaticus | - |
ADP + phosphate + succinyl-CoA | - |
r | |
6.2.1.4 | GTP + succinate + CoA | Thermus aquaticus | GTP is the preferred cosubstrate | GDP + phosphate + succinyl-CoA | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.2.1.4 | Thermus aquaticus | - |
- |
- |
EC Number | Renatured (Comment) | Organism |
---|---|---|
6.2.1.4 | denaturing of the enzyme in 6 M guanidinium chloride for 24 h and refolding by rapid dilution (1:20 v:v) into one of three solutions: benign buffer consisting of 50 mM KCl, 60 mM potassium phosphate pH 7.4, arginine buffer containing 0.67 M L-arginine-HCl, 60 mM potassium phosphate, pH 7.4, or arginine buffer containing 0.67 M L-arginine-HCl, 60 mM potassium phosphate, 50 mM Tris-HCl, pH 8.0, kinetics of refolding, overview. Enzyme refolding in arginine buffer, pH 7.4, is temperature-dependent, the rate of refolding follows apparent first-order kinetics. Omission of phosphate from the buffer does not affect the rate. The refolded enzyme form is much less thermostable than the native form | Thermus aquaticus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.4 | ATP + succinate + CoA | - |
Thermus aquaticus | ADP + phosphate + succinyl-CoA | - |
r | |
6.2.1.4 | GTP + succinate + CoA | GTP is the preferred cosubstrate | Thermus aquaticus | GDP + phosphate + succinyl-CoA | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.2.1.4 | heterotetramer | alpha2beta2 | Thermus aquaticus |
6.2.1.4 | More | structure comparisons, overview | Thermus aquaticus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.2.1.4 | SCS | - |
Thermus aquaticus |
6.2.1.4 | Succinyl-CoA synthetase | - |
Thermus aquaticus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.2.1.4 | 65 | - |
- |
Thermus aquaticus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.2.1.4 | 8 | 8.4 | - |
Thermus aquaticus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.4 | ADP | the enzyme either ADP/ATP or GDP/GTP, but prefers GDP/GTP | Thermus aquaticus | |
6.2.1.4 | ATP | the enzyme either ADP/ATP or GDP/GTP, but prefers GDP/GTP | Thermus aquaticus | |
6.2.1.4 | GDP | the enzyme either ADP/ATP or GDP/GTP, but prefers GDP/GTP | Thermus aquaticus | |
6.2.1.4 | GTP | the enzyme either ADP/ATP or GDP/GTP, but prefers GDP/GTP | Thermus aquaticus | |
6.2.1.4 | additional information | nucleotide-binding site, binding structure crystal structure analysis, modling, detailed overview | Thermus aquaticus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.2.1.4 | additional information | a water molecule and Pro20beta in Thermus aquaticus interact well with the guanine base and other residues of the nucleotide-binding site leading to the preference for GDP/GTP, but does not hinder the binding of ADP/ATP. Active site and succinate binding site structure analysis, overview | Thermus aquaticus |