EC Number   |
General Information |
Reference |
|---|
    4.2.1.2 | malfunction |
fumarase activity in extracts of leaves of fum2 mutants is reduced by approximately 85% relative to the wild-type. In the fum2-1 mutant, fumarate is present at a 10fold lower level and malate at a 2fold higher level than in the wild-type. Fum2-1 plants accumulate twice as much starch as the wild-type |
706242 |
| 4.2.1.2 | malfunction |
in the absence of cytosolic fumarate hydratase, the cellular response to DNA damage is impaired |
706404 |
| 4.2.1.2 | malfunction |
increased sensitivity (10-100fold) of the FUM1 mutant strain to ionizing radiation, to the presence of hydroxyurea and to double-strand breaks when compared to the wild-type. Cytosolic absence of fumarase in yeast with a DELTAfum1 chromosomal deletion can be complemented by human fumarase. Fumaric acid (25 mM) complements the phenotype of fumarase cytosolic absence. FUM1 mutant strain sensitivity to double-strand breaks can be complemented by catalytically active pDELTAMTS-FUM1 but not by the corresponding H153R mutant |
706404 |
| 4.2.1.2 | malfunction |
isolation of homozygous fum1 knock-out plants from self-fertilized heterozygotes is failing |
706242 |
| 4.2.1.2 | malfunction |
re-expression of cytosolic fumarate hydratase in FH1-deficient mice is critical for the suppression of renal cyst development and restoration of defects in the arginine biosynthesis pathway. fumarate hydratase-deficient cells exhibit a greater dependence on exogenous arginine than wild-type counterparts |
729549 |
| 4.2.1.2 | metabolism |
fumarase catalyzes the reversible hydration of fumarate to L-malate and is a key enzyme in the tricarboxylic acid cycle and in amino acid metabolism |
716122 |
| 4.2.1.2 | metabolism |
mesaconase activity of the promiscuous fumarase/mesaconase 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 |
-, 746828 |
| 4.2.1.2 | metabolism |
the enzyme participates in the methylaspartate pathway of glutamate fermentation as well as in the metabolism of various C5-dicarboxylic acids such as mesaconate or L-threo-beta-methylmalate. fumD is clustered with the key genes for two enzymes of the methylaspartate pathway of glutamate fermentation, glutamate mutase and methylaspartate ammonia lyase, converting glutamate to mesaconate |
-, 749072 |
| 4.2.1.2 | metabolism |
the enzyme probably plays a role in amino acid synthesis when the organism grows on carbohydrates |
745719 |
| 4.2.1.2 | physiological function |
cytosolic fumarase plays a role in the cellular response to double-strand breaks. Fumarase enzymatic activity is required for its DNA damage protective function. Fumarase activity is also required for the extra-mitochondrial function of fumarase |
706404 |
