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Literature summary for 4.2.1.2 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
Search for more literature for 4.2.1.2

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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