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Literature summary for 6.2.1.4 extracted from

  • Huang, J.; Fraser, M.
    Structural basis for the binding of succinate to succinyl-CoA synthetase (2016), Acta Crystallogr. Sect. D, 72, 912-921 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Sus scrofa

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with succinate, magnesium ions and CoA, hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3350 and 0.2 M magnesium formate Sus scrofa

Protein Variants

Protein Variants Comment Organism
V330M the mutant exhibits an about 10fold higher Km value for succinate compared to the wild type enzyme Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.49
-
succinate wild type enzyme, at pH 7.4 and 21°C Sus scrofa
5.1
-
succinate mutant enzyme V330M, at pH 7.4 and 21°C Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + succinate + CoA Sus scrofa
-
GDP + phosphate + succinyl-CoA
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa P53590
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, HiTrap Blue column chromatography, and Sephadex G-25 gel filtration Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + L-malate + CoA low activity Sus scrofa GDP + phosphate + L-malyl-CoA
-
?
GTP + succinate + CoA
-
Sus scrofa GDP + phosphate + succinyl-CoA
-
?
additional information no activity with citrate, fumarate and oxaloacetate Sus scrofa ?
-
?

Synonyms

Synonyms Comment Organism
GTP-specific succinyl-CoA synthetase
-
Sus scrofa
GTPSCS
-
Sus scrofa
SUCLG2
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
GTP
-
Sus scrofa