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Literature summary for 6.2.1.4 extracted from

  • Li, X.; Wu, F.; Beard, D.A.
    Identification of the kinetic mechanism of succinyl-CoA synthetase (2013), Biosci. Rep., 33, 145-163.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic mechanism and thermodynamic parameter values, quasi-steady-state models, evaluation of five different proposed mechanisms, overview. The ordered ter-ter mechanism with dead-end product inhibition of succinate against succinyl-CoA effectively matches kinetic data on pig heart enzyme, thermodynamic-constrained kinetic model 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
-
 r

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA catalytic mechanism Sus scrofa
a

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + succinate + CoA
-
 Sus scrofa GDP + phosphate + succinyl-CoA
-
 r

Synonyms

Synonyms Comment Organism
SCS
-
 Sus scrofa
Succinyl-CoA synthetase
-
 Sus scrofa
succinyl-coenzyme A synthetase
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
GDP
-
 Sus scrofa
GTP
-
 Sus scrofa

General Information

General Information Comment Organism
physiological function the enzyme participates in the tricarboxylic acid cycle, ketone body metabolism and haem biosynthesis Sus scrofa