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
-
uterine
-
leiomyoma
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hlrcc
-
germline
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isocitrate
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citrate
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tca
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papillary
-
krebs
-
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
-
analysis
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2-hydroxyglutarate
-
synthesis
-
papules
-
oncocytomas
-
medicine
-
industry
- 4.2.1.2
- succinate
- leiomyomatosis
- hereditary
-
tricarboxylic
- uterine
- leiomyoma
-
hlrcc
-
germline
- isocitrate
- citrate
- tca
-
papillary
-
krebs
- aconitase
- carboxylase
-
citric
-
predisposition
- fibroids
- phosphoenolpyruvate
- succinyl-coa
- nucleoli
-
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
ECTree
4.2.1.2 fumarate hydrataseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.2.1.2 - fumarate hydratase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-citramalate
mesaconate + H2O
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
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-
r
(S)-malate
fumarate + H2O
-
-
wild-type enzyme is rate-limited in the recycling of free enzyme isoforms that follows product release
?
(S)-malate
fumarate + H2O
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
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-
r
(S)-malate
fumarate + H2O
-
-
wild-type enzyme is rate-limited in the recycling of free enzyme isoforms that follows product release
?
fumarate + H2O
(S)-malate
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
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-
r
fumarate + H2O
(S)-malate
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
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-
r
fumarate + H2O
(S)-malate
Escherichia coli K-12 W3110 / K-12
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
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-
r
fumarate + H2O
(S)-malate
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heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
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-
r
fumarate + H2O
(S)-malate
Escherichia coli O157:H7 ATCC 700728
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heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
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-
r
fumarate + H2O
L-malate
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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
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?
fumarate + H2O
L-malate
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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
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?
fumarate + H2O
L-malate
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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
-
?
mesaconate + H2O
(S)-citramalate
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
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-
r
mesaconate + H2O
(S)-citramalate
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
mesaconate + H2O
(S)-citramalate
Escherichia coli K-12 W3110 / K-12
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
mesaconate + H2O
(S)-citramalate
-
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
mesaconate + H2O
(S)-citramalate
Escherichia coli O157:H7 ATCC 700728
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heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
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-
r
mesaconate + H2O
(S)-citramalate
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
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-
?
additional information
?
-
fumarate hydratase activity is favored over the malate dehydratase activity. Presence of oxalacetate, glutamine, and/or asparagine cause the malate dehydratase reaction to become preferred over the fumarate hydratase reaction
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-
?
additional information
?
-
fumarate hydratase activity is favored over the malate dehydratase activity. Presence of oxalacetate, glutamine, and/or asparagine cause the malate dehydratase reaction to become preferred over the fumarate hydratase reaction
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-
?
additional information
?
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-
fumarate hydratase activity is favored over the malate dehydratase activity. Presence of oxalacetate, glutamine, and/or asparagine cause the malate dehydratase reaction to become preferred over the fumarate hydratase reaction
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-
?
additional information
?
-
fumarate hydratase activity is favored over the malate dehydratase activity. Presence of oxaloacetate, glutamine, and/or asparagine cause the malate dehydratase reaction to become preferred over the fumarate hydratase reaction
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-
?
additional information
?
-
fumarate hydratase activity is favored over the malate dehydratase activity. Presence of oxaloacetate, glutamine, and/or asparagine cause the malate dehydratase reaction to become preferred over the fumarate hydratase reaction
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-
?
additional information
?
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-
fumarate hydratase activity is favored over the malate dehydratase activity. Presence of oxaloacetate, glutamine, and/or asparagine cause the malate dehydratase reaction to become preferred over the fumarate hydratase reaction
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-
?
additional information
?
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-
stimulation of fumarase synthesis by changing medium components
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-
?
additional information
?
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enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
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-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
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-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
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-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
-
-
?
additional information
?
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-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
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-
?
additional information
?
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-
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
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-
?
additional information
?
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-
germline mutations in fumarate hydratase gene at 1q43 predispose to hereditary leiomyomatosis and renal cell cancer (HLRCC) syndrome. In HLRCC, the most common clinical features are leiomyomas of the skin and uterus, and in a subset of the families, renal cell cancer (RCC) and uterine leiomyosarcoma (ULMS) occur frequently at young age. On the population level hereditary FH defects do play a role in pathogenesis of sporadic early onset ULMSs, albeit rarely
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-
?
additional information
?
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hereditary leiomyomatosis and renal cell cancer is a hereditary cancer syndrome predisposing individuals to the development of aggressive kidney cancer. These individuals harbour a germline mutation of fumarate hydratase
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-
?
additional information
?
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Leydig cell tumors are caused by fumarate hydratase mutations
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?
additional information
?
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tumorigenic effect of fumarate hydratase mutations involve more than one mechanism
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?
additional information
?
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fumarate hydratase is a key enzyme of the tricarboxylic cycle
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?
additional information
?
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hypoxia activation due to fumarate accumulation may be a tissue-specific response
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?
additional information
?
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no activity with either mesaconate or (S)-citramalate
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-
?
additional information
?
-
no activity with either mesaconate or (S)-citramalate
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-
?
additional information
?
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-
no activity with either mesaconate or (S)-citramalate
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-
?
additional information
?
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Paraburkholderia xenovorans DSMZ 17367 / LB400
no activity with either mesaconate or (S)-citramalate
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-
?
additional information
?
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Paraburkholderia xenovorans DSMZ 17367 / LB400
no activity with either mesaconate or (S)-citramalate
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-
?
additional information
?
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Paraburkholderia xenovorans DSMZ 17367 / LB400
no substrate: mesaconate
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-
?
additional information
?
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Paraburkholderia xenovorans DSMZ 17367 / LB400
no substrate: mesaconate
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-
?
additional information
?
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-
the iron-regulated tricarboxylic acid cycle enzyme fumarase C is essential for optimal alginate production by Pseudomonas aeruginosa
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-
?
additional information
?
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no activity with D-malate, maleate, citramalate and citrate
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-
?
additional information
?
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-
no activity with D-malate, maleate, citramalate and citrate
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-
?
