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Literature summary extracted from

  • Flint, D.H.
    Initial kinetic and mechanistic characterization of Escherichia coli fumarase A (1994), Arch. Biochem. Biophys., 311, 509-516.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.2 (-)-citramalate no inhibition by (+)-citramalate Escherichia coli
4.2.1.2 (2R,3R)-Tartrate
-
 Escherichia coli
4.2.1.2 2-hydroxy-3-nitropropionate nitronate form Escherichia coli
4.2.1.2 chlorofumarate
-
 Escherichia coli
4.2.1.2 cis-aconitate
-
 Escherichia coli
4.2.1.2 citraconate
-
 Escherichia coli
4.2.1.2 citrate
-
 Escherichia coli
4.2.1.2 DL-3-phenyllactate
-
 Escherichia coli
4.2.1.2 meso-tartrate
-
 Escherichia coli
4.2.1.2 trans-aconitate
-
 Escherichia coli
4.2.1.2 trans-glutaconate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.2 0.6
-
 fumarate fumarase A Escherichia coli
4.2.1.2 0.7
-
 (S)-malate fumarase A Escherichia coli
4.2.1.2 0.9
-
 acetylene dicarboxylate
-
 Escherichia coli
4.2.1.2 1.7
-
 fluorofumarate
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.2 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.2 (S)-malate
-
 Escherichia coli fumarate + H2O
-
 r
4.2.1.2 2(S)-3(S)-tartrate
-
 Escherichia coli oxaloacetate
-
 ?
4.2.1.2 acetylene dicarboxylate + H2O
-
 Escherichia coli oxaloacetate
-
 ?
4.2.1.2 alpha-fluorofumarate + H2O
-
 Escherichia coli oxaloacetate + ?
-
 ?
4.2.1.2 fluorofumarate + H2O
-
 Escherichia coli ?
-
 ?
4.2.1.2 fumarate + H2O
-
 Escherichia coli L-malate
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.2 additional information
-
 additional information
-
 Escherichia coli
4.2.1.2 11.2
-
 (S)-malate fumarase A Escherichia coli
4.2.1.2 51.7
-
 fumarate fumarase A Escherichia coli