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Literature summary extracted from

  • Kurz, L.C.; Shah, S.; Frieden, C.; Nakra, T.; Stein, R.E.; Drysdale, G.R.; Evans, C.T.; Srere, P.A.
    Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site (1995), Biochemistry, 34, 13278-13288.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.3.1 H320G effect of H320G substitution, solvent accessibility, and conformational changes on catalysis and activity Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.1 0.005
-
 acetyl-CoA wild-type Sus scrofa
2.3.3.1 0.0059
-
 oxaloacetate wild-type Sus scrofa
2.3.3.1 0.043
-
 oxaloacetate mutant H320G Sus scrofa
2.3.3.1 0.089
-
 acetyl-CoA mutant H320G Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.1 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.3.1 acetyl-CoA + H2O + oxaloacetate = citrate + CoA mechanism Sus scrofa
a
2.3.3.1 acetyl-CoA + H2O + oxaloacetate = citrate + CoA active site His320 Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.3.1 heart
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.3.1 additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.1 acetyl-CoA + oxaloacetate + H2O intermediate citryl-CoA Sus scrofa citrate + CoA
-
 r

Subunits

EC Number Subunits Comment Organism
2.3.3.1 More molecular basis of subunit interactions Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.3.1 0.275
-
 oxaloacetate mutant H320G Sus scrofa
2.3.3.1 167
-
 oxaloacetate wild-type Sus scrofa