4.2.1.2: fumarate hydratase
This is an abbreviated version!
For detailed information about fumarate hydratase, go to the full flat file.
Word Map on EC 4.2.1.2
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4.2.1.2
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succinate
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leiomyomatosis
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hereditary
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tricarboxylic
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uterine
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leiomyoma
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hlrcc
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germline
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isocitrate
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citrate
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tca
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papillary
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krebs
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aconitase
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carboxylase
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citric
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predisposition
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fibroids
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phosphoenolpyruvate
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succinyl-coa
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nucleoli
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l-malic
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halo
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alpha-ketoglutarate
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leiomyosarcoma
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oncometabolite
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paragangliomas
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aspartase
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pseudohypoxic
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reed
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oxalacetate
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perinucleolar
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hippel-lindau
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hysterectomy
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chromophobe
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1.1.1.37
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analysis
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2-hydroxyglutarate
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synthesis
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papules
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oncocytomas
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medicine
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industry
- 4.2.1.2
- succinate
- leiomyomatosis
- hereditary
-
tricarboxylic
- uterine
- leiomyoma
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hlrcc
-
germline
- isocitrate
- citrate
- tca
-
papillary
-
krebs
- aconitase
- carboxylase
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citric
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predisposition
- fibroids
- phosphoenolpyruvate
- succinyl-coa
- nucleoli
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l-malic
-
halo
- alpha-ketoglutarate
- leiomyosarcoma
-
oncometabolite
- paragangliomas
- aspartase
-
pseudohypoxic
-
reed
- oxalacetate
-
perinucleolar
-
hippel-lindau
-
hysterectomy
-
chromophobe
-
1.1.1.37
- analysis
- 2-hydroxyglutarate
- synthesis
-
papules
- oncocytomas
- medicine
- industry
Reaction
Synonyms
At2g47510, At5g50950, Bxe_A1038, Bxe_A3136, class II fumarase, Fum, FUM C, FUM1, FUM2, FumA, fumarase, fumarase A, fumarase C, fumarase/mesaconase, fumarate hydratase, FumB, FumC, FumD, FumF, FUMR, hydratase, fumarate, L-malate hydro-lyase, LmFH-1, LmFH-2, LmjF24.0320, LmjF29.1960, mesaconase/fumarase, MmcBC, PF1754, PF1755, rv1098c, scFUMC, slFumC, stFUMC, Tneu_1334, Tneu_1335
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General Information
General Information on EC 4.2.1.2 - fumarate hydratase
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malfunction
metabolism
physiological function
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
malfunction
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in the absence of cytosolic fumarate hydratase, the cellular response to DNA damage is impaired
malfunction
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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
malfunction
isolation of homozygous fum1 knock-out plants from self-fertilized heterozygotes is failing
malfunction
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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
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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
metabolism
Q8U062; Q8U063
the enzyme probably plays a role in amino acid synthesis when the organism grows on carbohydrates
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
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
metabolism
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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
metabolism
Paraburkholderia xenovorans DSMZ 17367 / LB400
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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
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metabolism
Escherichia coli K-12 W3110 / K-12
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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
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metabolism
Escherichia coli O157:H7 ATCC 700728
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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
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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
physiological function
FUM1 is an essential enzyme, consistent with its role in the tricarboxylic acid cycle
physiological function
FUM2 accounts for much more activity than FUM1 in leaves. FUM2 is not required for seed germination and seedling growth. FUM2 is required for fumarate accumulation from malate in leaves. Accumulation of fumarate catalysed by FUM2 is required for effective assimilation of nitrogen and growth on high nitrogen
physiological function
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fumarase in permeabilized non-growing cells used as biocatalysts for continuous production of L-malic acid
physiological function
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fumarase in permeabilized non-growing cells used as biocatalysts for continuous production of L-malic acid
physiological function
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fumarate hydratase and fumaric acid are critical elements of the DNA damage response, which underlies the tumor suppressor role of fumarate hydratase and which is most probably independent of hypoxia-inducible factor. Cytoplasmic version of fumarate hydratase has a role in repairing DNA double-strand breaks in the nucleus. This role involves the movement of fumarate hydratase from the cytoplasm into the nucleus and depends on its enzymatic activity. When fumarate hydratase is absent from cells, its function in DNA repair can be substituted by high concentrations of one of the enzyme's products, fumaric acid. Fumarate hydratase deficiency leads to cancer because there is not enough fumaric acid in the nucleus to stimulate repair of DNA double-strand breaks. Can complement the cytosolic absence of fumarase in yeast with a DELTAfum1 chromosomal deletion
physiological function
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metabolites of the glyoxylate shunt act as nanosensors for fumarase subcellular targeting and distribution. Glyoxylate shunt deletion mutants exhibit an altered fumarase dual distribution. Expression levels of Cit2 affect dual targeting of fumarase. Amount of cytosolic fumarase is drastically reduced in the DELTAcit2 strain, when compared with the wild-type strain. Proportion of fumarase activity is very low in the cytosolic versus mitochondrial fractions obtained from DELTAcit2 and wild-type plus pCit2 strains when compared with the wild-type or DELTAcit2 plus pCit2 strains, in which the fumarase activity is divided equally between the corresponding subcellular fractions
physiological function
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presence of lysine at amino acid position 481 in Dahl salt-sensitive rats and glutamic acid in Brown Norway and SS-13BN rats. The variation K481E likely contributes to the much higher specific activity of fumarase in SS-13BN rats. Total fumarase activity is significantly lower in the kidneys of Dahl salt-sensitive rats compared with SS-13BN rats, despite an apparent compensatory increase in fumarase abundance in Dahl salt-sensitive rats
physiological function
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purified fumarase used as biocatalysts for continuous production of L-malic acid
physiological function
fumarase catalyzes the reversible hydration of fumarate to L-malate in Rhizopus oryzae
physiological function
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enzyme is required for the DNA damage response. Fumarase-dependent intracellular signaling of the Bacillus subtilis DNA damage response is achieved via production of L-malic acid, which affects the translation of RecN, the first protein recruited to DNA damage sites. Absence of fumarase in the bacterial cell affects the levels and localization of the DNA damage response protein RecN. Expression in a mutant yeast strain can complement the lack of extra-mitochondrial fumarase with respect to sensitivity to DNA damage
physiological function
Paraburkholderia xenovorans is able to grow on itaconate and mesaconate (i.e. methylfumarate). Mesaconate is metabolized through its hydration to (S)-citramalate, which is then metabolized to acetyl-CoA and pyruvate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by class I fumarase Bxe_A3136
physiological function
plants of T-DNA insertion mutants, lacking isoform Fum2, show marked differences in their response to cold. The Fum2 mutant plants accumulate higher concentrations of phosphorylated sugar intermediates and of starch and malate. Transcripts for proteins involved in photosynthesis are markedly down-regulated in the mutant plants but not in wild-type Columbia-0. Mutant plants show a complete loss of the ability to acclimate photosynthesis to low temperature
physiological function
the enzyme (Bxe_A3136) is in fact a promiscuous fumarase/mesaconase. It has similar efficiencies (kcat/Km) for both fumarate and mesaconate hydration. This promiscuity is physiologically relevant, as it allows the growth of this bacterium on mesaconate as a sole carbon and energy source
physiological function
Paraburkholderia xenovorans DSMZ 17367 / LB400
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Paraburkholderia xenovorans is able to grow on itaconate and mesaconate (i.e. methylfumarate). Mesaconate is metabolized through its hydration to (S)-citramalate, which is then metabolized to acetyl-CoA and pyruvate. The first reaction of the pathway, the mesaconate hydratase (mesaconase) reaction, is catalyzed by class I fumarase Bxe_A3136
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physiological function
Paraburkholderia xenovorans DSMZ 17367 / LB400
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the enzyme (Bxe_A3136) is in fact a promiscuous fumarase/mesaconase. It has similar efficiencies (kcat/Km) for both fumarate and mesaconate hydration. This promiscuity is physiologically relevant, as it allows the growth of this bacterium on mesaconate as a sole carbon and energy source
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