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Literature summary for 4.2.1.2 extracted from

  • Woods, S.A.; Schwartzbach, S.D.; Guest, J.R.
    Two biochemically distinct classes of fumarase in Escherichia coli (1988), Biochim. Biophys. Acta, 954, 14-26.
    View publication on PubMed
Search for more literature for 4.2.1.2

General Stability

General Stability Organism
enzyme form FUMB is extremely unstable Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
 fumarate enzyme form FUMA Escherichia coli
0.39
-
 fumarate enzyme form FUMC Escherichia coli
0.63
-
 (S)-malate enzyme form FUMB Escherichia coli
1.1
-
 (S)-malate enzyme form FUMA Escherichia coli
1.7
-
 fumarate enzyme form FUMB Escherichia coli
2.94
-
 L-malate enzyme form FUMC Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 4 * 50000, enzyme form FUMC, SDS-PAGE Escherichia coli
61000
-
 2 * 61000, enzyme form FUMA, SDS-PAGE Escherichia coli
120000
-
 enzyme form FUMA, gel filtration Escherichia coli
200000
-
 enzyme form FUMC, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 3 fumarases FUMA, FUMB, and FUMC
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate
-
 Escherichia coli fumarate + H2O
-
 r
fumarate + H2O
-
 Escherichia coli L-malate
-
 r

Subunits

Subunits Comment Organism
dimer 2 * 61000, enzyme form FUMA, SDS-PAGE Escherichia coli
tetramer 4 * 50000, enzyme form FUMC, SDS-PAGE Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 80 min, 30% loss of activity of the enzyme form FUMC. Rapid inactivation of enzyme form FUMA and FUMB Escherichia coli