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Literature summary for 2.3.3.1 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
Search for more literature for 2.3.3.1

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More molecular basis of subunit interactions Sus scrofa

Turnover Number [1/s]

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