EC Number   |
Natural Substrates |
|---|
    4.2.1.2 | (S)-malate |
- |
| 4.2.1.2 | fumarate + H2O |
constitutive enzyme |
| 4.2.1.2 | fumarate + H2O |
enzyme of Krebs cycle |
| 4.2.1.2 | fumarate + H2O |
Fum A and FumC activities are induced 4fold to 5fold when the cell growth rate is lowered from 1.2/h to 0.24/h at 1% and 21% O2. Twofold induction of FumA and FumC activities when acetate is utilized instead of glucose as the sole carbon source. Growth rate control of FumA and FumC activities is cAMP dependent. While FumB activity is maximal during anaerobic groth, FumA is the major enzyme under anaerobic cell growth, and the maximal activity is achieved when oxygen is elevated to 1-2%. Further increrase in oxygen level causes inactivation of FumA and FumB activities |
| 4.2.1.2 | fumarate + H2O |
in CAM plants fumarase is much lower than in C3 plants. Under low light and prolonged salt treatment, an increase of fumarase activity is detected. This change is not observed at high light |
| 4.2.1.2 | mesaconate + H2O |
- |
| 4.2.1.2 | mesaconate + H2O |
mesaconase activity of class I fumarase contributes to mesaconate utilization by Burkholderia xenovorans. Mesaconate is metabolized through its hydration to (S)-citramalate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by a class I fumarase. The latter compound is then metabolized to acetyl-CoA and pyruvate with the participation of two enzymes of the itaconate degradation pathway, a promiscuous itaconate-CoA transferase able to activate (S)-citramalate in addition to itaconate and (S)-citramalyl-CoA lyase |
| 4.2.1.2 | more |
enzyme of the tricarboxylic acid cycle |
| 4.2.1.2 | more |
the iron-regulated tricarboxylic acid cycle enzyme fumarase C is essential for optimal alginate production by Pseudomonas aeruginosa |
| 4.2.1.2 | more |
all missense mutations of fumarate hydratase associating with MCUL/hereditary leiomyomatosis and renal cell cancer show diminished fumarate hydratase enzymatic. It is suggested that the tumor suppressor role of fumarate hydratase may relate to its enzymatic function |
