Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Joyce, M.A.; Hayakawa, K.; Wolodko, W.T.; Fraser, M.E.
    Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus (2012), Acta Crystallogr. Sect. D, 68, 751-762.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.4 Thermus aquaticus
-
-
-

Renatured (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
6.2.1.4 heterotetramer alpha2beta2 Thermus aquaticus
6.2.1.4 More structure comparisons, overview Thermus aquaticus

Synonyms

EC Number Synonyms Comment Organism
6.2.1.4 SCS
-
Thermus aquaticus
6.2.1.4 Succinyl-CoA synthetase
-
Thermus aquaticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.4 65
-
-
Thermus aquaticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.4 8 8.4
-
Thermus aquaticus

Cofactor

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

General Information

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