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(2S,3S)-tartrate
oxaloacetate + H2O
(S)-citramalate
mesaconate + H2O
(S)-malate
fumarate + H2O
(S,S)-tartrate
oxaloacetate + H2O
2(S)-3(S)-tartrate
oxaloacetate
-
-
-
?
acetylene dicarboxylate + H2O
oxaloacetate
alpha-fluorofumarate + H2O
oxaloacetate + ?
bromofumarate + H2O
?
-
-
-
-
?
chlorofumarate + H2O
?
-
-
-
-
?
fumarate + H2O
(S)-malate
fumaric acid + H2O
(S)-malic acid
-
-
-
-
?
fumaric acid + H2O
L-malic acid
-
-
-
-
?
iodofumarate + H2O
?
-
-
-
-
?
L-tartrate
oxaloacetate + H2O
-
-
-
?
L-threo-chloro-L-malate
chlorofumarate + H2O
-
-
-
?
L-threo-hydroxyaspartate
?
-
-
-
-
?
mesaconate + H2O
(S)-citramalate
mesaconate + H2O
?
-
-
-
-
?
additional information
?
-
(2S,3S)-tartrate
oxaloacetate + H2O
-
-
-
?
(2S,3S)-tartrate
oxaloacetate + H2O
-
-
-
?
(2S,3S)-tartrate
oxaloacetate + H2O
-
-
-
?
(2S,3S)-tartrate
oxaloacetate + H2O
-
-
-
-
?
(2S,3S)-tartrate
oxaloacetate + H2O
-
-
-
-
?
(S)-citramalate
mesaconate + H2O
-
-
-
r
(S)-citramalate
mesaconate + H2O
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
-
-
r
(S)-citramalate
mesaconate + H2O
-
-
-
r
(S)-citramalate
mesaconate + H2O
-
-
-
r
(S)-citramalate
mesaconate + H2O
-
-
-
-
r
(S)-citramalate
mesaconate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
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
-
-
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
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
Q8U062; Q8U063
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
-
?
(S)-malate
fumarate + H2O
-
-
-
?
(S,S)-tartrate
oxaloacetate + H2O
-
-
-
?
(S,S)-tartrate
oxaloacetate + H2O
-
-
-
?
acetylene dicarboxylate + H2O
oxaloacetate
-
-
-
?
acetylene dicarboxylate + H2O
oxaloacetate
-
-
-
?
alpha-fluorofumarate + H2O
oxaloacetate + ?
-
-
-
?
alpha-fluorofumarate + H2O
oxaloacetate + ?
-
-
-
-
?
D-tartrate
?
-
-
-
-
?
D-tartrate
?
Q8U062; Q8U063
-
-
-
?
fluorofumarate + H2O
?
-
-
-
-
?
fluorofumarate + H2O
?
-
-
-
-
?
fumarate + H2O
(S)-malate
-
-
-
r
fumarate + H2O
(S)-malate
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
-
-
r
fumarate + H2O
(S)-malate
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
fumarate + H2O
(S)-malate
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
fumarate + H2O
(S)-malate
-
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
fumarate + H2O
(S)-malate
-
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
fumarate + H2O
(S)-malate
-
-
-
r
fumarate + H2O
(S)-malate
Q8U062; Q8U063
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
constitutive enzyme
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
constitutive enzyme
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
constitutive enzyme
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
enzyme of Krebs cycle
-
r
fumarate + H2O
L-malate
-
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
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
enzyme of Krebs cycle
-
r
fumarate + H2O
L-malate
-
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
-
?
fumarate + H2O
L-malate
-
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
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
-
?
fumarate + H2O
L-malate
-
-
-
r
fumarate + H2O
L-malate
-
-
-
r
L-malate
fumarate + H2O
-
-
-
r
L-malate
fumarate + H2O
-
-
-
-
r
L-malate
fumarate + H2O
-
-
-
r
L-malate
fumarate + H2O
-
-
-
r
L-malate
fumarate + H2O
-
-
-
?
L-malate
fumarate + H2O
-
-
-
?
L-malate
fumarate + H2O
-
-
-
r
L-malate
fumarate + H2O
-
-
-
r
L-malate
fumarate + H2O
-
-
-
?
L-malate
fumarate + H2O
-
-
-
?
mesaconate + H2O
(S)-citramalate
-
-
-
r
mesaconate + H2O
(S)-citramalate
the catalytic efficiency of FumA with (S)-citramalate/mesaconate is about 4% of that with fumarate or (S)-malate
-
-
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
heterologously produced FumD is a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate
-
-
r
mesaconate + H2O
(S)-citramalate
-
-
-
-
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
-
-
-
-
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
-
-
-
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
-
-
?
S-malate
fumarate + H2O
-
-
-
-
?
S-malate
fumarate + H2O
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
stimulation of fumarase synthesis by changing medium components
-
-
?
additional information
?
-
almost no activity with mesaconate
-
-
?
additional information
?
-
almost no activity with mesaconate
-
-
?
additional information
?
-
almost no activity with mesaconate
-
-
?
additional information
?
-
almost no activity with mesaconate
-
-
?
additional information
?
-
-
almost no activity with mesaconate
-
-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
-
-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
-
-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
-
-
?
additional information
?
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
-
-
?
additional information
?
-
-
enzyme is a promiscuous mesaconase/fumarase with a 2- to 3fold preference for mesaconate over fumarate
-
-
?
additional information
?
-
almost no activity with mesaconate
-
-
?
additional information
?
-
almost no activity with mesaconate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Leydig cell tumors are caused by fumarate hydratase mutations
-
-
?
additional information
?
-
-
tumorigenic effect of fumarate hydratase mutations involve more than one mechanism
-
-
?
additional information
?
-
-
fumarate hydratase is a key enzyme of the tricarboxylic cycle
-
-
?
additional information
?
-
-
hypoxia activation due to fumarate accumulation may be a tissue-specific response
-
-
?
additional information
?
-
no activity with either mesaconate or (S)-citramalate
-
-
?
additional information
?
-
no activity with either mesaconate or (S)-citramalate
-
-
?
additional information
?
-
-
no activity with either mesaconate or (S)-citramalate
-
-
?
additional information
?
-
no substrate: mesaconate
-
-
?
additional information
?
-
no substrate: mesaconate
-
-
?
additional information
?
-
-
no substrate: mesaconate
-
-
?
additional information
?
-
no activity with either mesaconate or (S)-citramalate
-
-
?
additional information
?
-
no activity with either mesaconate or (S)-citramalate
-
-
?
additional information
?
-
no substrate: mesaconate
-
-
?
additional information
?
-
no substrate: mesaconate
-
-
?
additional information
?
-
-
the iron-regulated tricarboxylic acid cycle enzyme fumarase C is essential for optimal alginate production by Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
no activity with D-malate, maleate, citramalate and citrate
-
-
?
additional information
?
-
-
no activity with D-malate, maleate, citramalate and citrate
-
-
?
additional information
?
-
-
enzyme of the tricarboxylic acid cycle
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-malate
fumarate + H2O
mesaconate + H2O
(S)-citramalate
additional information
?
-
(S)-malate
fumarate + H2O
-
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
r
(S)-malate
fumarate + H2O
-
-
-
-
r
fumarate + H2O
L-malate
-
constitutive enzyme
-
?
fumarate + H2O
L-malate
-
constitutive enzyme
-
?
fumarate + H2O
L-malate
-
constitutive enzyme
-
?
fumarate + H2O
L-malate
enzyme of Krebs cycle
-
r
fumarate + H2O
L-malate
-
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
-
?
fumarate + H2O
L-malate
-
enzyme of Krebs cycle
-
r
fumarate + H2O
L-malate
-
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
-
?
fumarate + H2O
L-malate
-
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
-
-
-
-
r
mesaconate + H2O
(S)-citramalate
-
-
-
-
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
-
-
?
additional information
?
-
-
stimulation of fumarase synthesis by changing medium components
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Leydig cell tumors are caused by fumarate hydratase mutations
-
-
?
additional information
?
-
-
tumorigenic effect of fumarate hydratase mutations involve more than one mechanism
-
-
?
additional information
?
-
-
fumarate hydratase is a key enzyme of the tricarboxylic cycle
-
-
?
additional information
?
-
-
hypoxia activation due to fumarate accumulation may be a tissue-specific response
-
-
?
additional information
?
-
-
the iron-regulated tricarboxylic acid cycle enzyme fumarase C is essential for optimal alginate production by Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
enzyme of the tricarboxylic acid cycle
-
-
?
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Ca2+
has a small stimulatory effect
Fe
-
enzyme contains an oxygen-sensitive [4Fe-4S] cluster
[3Fe-4S] center
-
10-25% of purified protein contains [3Fe-4S] cluster
Fe2+
-
aerobic purification results in inactive protein, which can only partly be reactivated with Fe2+ and thiol
Fe2+
storage of the protein for 6 months leads to almost complete loss of its activity, which can be fully restored by the reactivation with Fe2+ and thiol
Iron
-
one Fe-S-dependent enzyme form and one Fe-S-independent enzyme form
Iron
-
in cells grown without aeration the Fe-S-independent enzyme form occupies over 80% of the overall fumarase. In aerobically grown cells the Fe-S-dependent fumarase occupies 80% of the overall activity
Iron
-
fumarase A contains a catalytically active [4Fe-4S]cluster
Iron
Q8U062; Q8U063
[4Fe-4S]-cluster containing heterodimeric enzyme
Mg2+
2 mM, slight stimulation
Mg2+
10fold activation of isoform Fum2
Mg2+
about 20fold activation of isoform Fum1
Mg2+
-
required, stimulates 10% at 5 mM
Mg2+
-
cytosolic form gets strongly activated, mitochondrial form only moderately activated
Mn2+
15fold activation of isoform Fum2
Mn2+
-
cytosolic form gets strongly activated, mitochondrial form only less effectively activated
additional information
activity does not increase upon incubation with Fe2+
additional information
activity does not increase upon incubation with Fe2+
additional information
activity does not increase upon incubation with Fe2+
additional information
activity does not increase upon incubation with Fe2+
additional information
-
activity does not increase upon incubation with Fe2+
additional information
not activating: Ca2+, K+
additional information
not activating: Ca2+, K+
additional information
not activating: Ca2+, K+, Mn2+
additional information
not activating: Ca2+, K+, Mn2+
additional information
-
aluminium and gallium do not perturb the activity of fumarase C
additional information
no effects of Zn2+, Fe2+, or EDTA on enzyme activity
additional information
-
class II fumarase activity is frequently influenced by divalent metal ions and non-ionic surfactants. No effect by Ca2+
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(-)-citramalate
-
no inhibition by (+)-citramalate
(R)-malate
mixed-type inhibition
2-hydroxy-3-nitropropionate
-
nitronate form
2-propanol
-
15-20% of maximum activity when assayed in 40% (v/v) 2-propanol
citrylpolymethylenediamine
-
-
-
CuCl2
-
inhibits 37% at 5 mM
Cyanate
-
2 mM ibuprofen and its major metabolites protect by up to 26%. Ibuprofen and the metabolites do not bind to fumarase
D-fructose
-
2 mM ibuprofen and its major metabolites protect by up to 26%. Ibuprofen and the metabolites do not bind to fumarase
EDTA
-
inhibits 20% at 2.5 mM
ethanol
-
15-20% of maximum activity when assayed in 40% (v/v) ethanol
FeCl2
-
inhibits 37% at 5 mM
FeCl3
-
inhibits 47.3% at 5 mM
fumarate
the activity of FUMR catalyzing hydration of fumarate to L-malate is completely inhibited by 2 mM fumaric acid
glycerol
-
wild-type enzyme is inhibited due to a viscogenic effect on the recycling rate
H2O2
-
causes fibril aggregation and catalytic inactivation of fumarase
hydroxyl radical
-
causes fibril aggregation and catalytic inactivation of fumarase
isocitrate
-
L-isocitrate
L-threo-hydroxyaspartate
-
-
mesotartaric acid
competitive
methanol
-
94% of maximum activity when assayed in 40% (v/v) methanol
NaCl
-
in cells cultivated with 200 mM NaCl, the inhibition produced in fumarase is 90%
NH4Cl
-
inhibits 23% at 5 mM
potassium thiocyanate
-
IC50: 140 mM
Prednisolone
-
2 mM ibuprofen and its major metabolites have no effect on prednisolone-induced inactivation
pyromellitate
competitive
S-2,3-dicarboxyaziridine
-
enzyme form FUMC is inhibited, enzyme form FUMA is not inhibited
ZnCl2
-
inhibits 55% at 5 mM
ATP
competitive or mixed-type inhibition
ATP
-
0.35 mM, 50% inhibition
chlorofumarate
-
-
citrate
-
meso-tartrate
competitive
phosphate
-
at 0.1 mM malate and 5 mM: 14% increase in activity. At 0.1 mM malate and 50 mM phosphate: 60% inhibition. At 1 mM malate and 10 mM phosphate: 80% stimulation
phosphate
-
increases activity at less than 5 mM, competitive inhibition at higher concentrations
sulfhydryl reagents
-
-
sulfhydryl reagents
-
no inhibition
trans-aconitate
-
-
additional information
no inactivation with L-tartrate, citrate, succinate, glycine, maleate, 1 mM iodoacetate, 1 mM iodoacetamide, 1 mM N-ethylmaleimide or 0.5 mM PCMB
-
additional information
-
no inactivation with L-tartrate, citrate, succinate, glycine, maleate, 1 mM iodoacetate, 1 mM iodoacetamide, 1 mM N-ethylmaleimide or 0.5 mM PCMB
-
additional information
-
inhibition by D2O arises in the recycling phase
-
additional information
-
no substrate inhibition by high levels of malate
-
additional information
-
during continuous L-malic acid production, enzyme inactivation, which is not complete
-
additional information
-
during continuous L-malic acid production, enzyme inactivation, which is not complete
-
additional information
-
substrate inhibition between 0.1 M and 1.0 M
-
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0.8 - 6.2
(2S,3S)-tartrate
0.52 - 1.08
(S)-citramalate
0.145 - 0.9
acetylene dicarboxylate
0.027 - 1.7
fluorofumarate
0.02 - 0.14
L-threo-chloromalate
-
-
7.5 - 10
L-threo-hydroxyaspartate
-
-
additional information
additional information
-
reaction kinetics and thermodynamics, overview
-
0.8
(2S,3S)-tartrate
pH 6.9, 37°C
2
(2S,3S)-tartrate
pH 6.9, 37°C
2.6
(2S,3S)-tartrate
-
pH 6.9, 37°C
6.2
(2S,3S)-tartrate
pH 6.9, 37°C
0.52
(S)-citramalate
pH 8.0, 30°C
0.52
(S)-citramalate
pH 6.9, 30°C
0.92
(S)-citramalate
-
pH 6.9, 37°C
0.92
(S)-citramalate
37°C, pH 6.9
1.04
(S)-citramalate
pH 6.9, 37°C
1.04
(S)-citramalate
37°C, pH 6.9
1.08
(S)-citramalate
pH 6.9, 37°C
1.08
(S)-citramalate
37°C, pH 6.9
0.12
(S)-malate
-
pH 6.5, 50 mM MOPS-NaOH buffer
0.14
(S)-malate
-
mitochondrial enzyme
0.2
(S)-malate
-
pH 6.9, 37°C
0.28
(S)-malate
pH 8.0, 30°C
0.3
(S)-malate
-
pH 7.5, 70°C
0.33
(S)-malate
-
pH 7.0, 50 mM MOPS-NaOH buffer
0.4
(S)-malate
pH 6.9, 37°C
0.41
(S)-malate
Q8U062; Q8U063
pH 8, 75°C
0.42
(S)-malate
pH 8.0, 30°C
0.46
(S)-malate
pH 7.4, 30°C, recombinant enzyme
0.59
(S)-malate
-
pH 7.0, 55°C
0.63
(S)-malate
-
enzyme form FUMB
0.7
(S)-malate
-
fumarase A
0.78
(S)-malate
pH 6.9, 37°C
0.93
(S)-malate
pH 6.9, 37°C
1
(S)-malate
-
pH 7.5, 50 mM MOPS-NaOH buffer
1.1
(S)-malate
-
enzyme form FUMA
1.22
(S)-malate
pH 7.3, 30°C, recombinant enzyme
1.4
(S)-malate
MES-NaOH buffer, pH 6.0
1.43
(S)-malate
pH 7.3, 30°C, worm enzyme
1.8
(S)-malate
MES-NaOH buffer, pH 7.0
1.8
(S)-malate
phosphate buffer, pH 6.0
2
(S)-malate
-
pH 6.5, 50 mM potassium phosphate buffer
5
(S)-malate
MES-NaOH buffer, pH 7.0
6.3
(S)-malate
phosphate buffer, pH 7.0
13
(S)-malate
phosphate buffer, pH 6.0
14
(S)-malate
-
pH 7.5, 50 mM potassium phosphate buffer
32
(S)-malate
-
pH 7.4, 37°C
0.8
(S,S)-Tartrate
37°C, pH 6.9
2
(S,S)-Tartrate
37°C, pH 6.9
2.6
(S,S)-Tartrate
37°C, pH 6.9
6.2
(S,S)-Tartrate
37°C, pH 6.9
0.145
acetylene dicarboxylate
-
-
0.9
acetylene dicarboxylate
-
-
0.51
D-Tartrate
Q8U062; Q8U063
pH 8, 75°C
0.7
D-Tartrate
-
pH 8, 37°C, Vmax: 2.3 micromol/minute/mg/
0.8
D-Tartrate
-
pH 8, 37°C, Vmax: 9.2 micromol/minute/mg/
0.027
fluorofumarate
-
-
0.005
fumarate
-
-
0.013
fumarate
-
cytosolic enzyme
0.094
fumarate
pH 6.9, 37°C
0.094
fumarate
37°C, pH 6.9
0.1
fumarate
pH 8.0, 30°C
0.1
fumarate
pH 6.9, 30°C
0.125
fumarate
-
pH 7.5, 70°C
0.138
fumarate
pH 8.0, 30°C
0.138
fumarate
pH 6.9, 30°C
0.15
fumarate
-
enzyme form FUMA
0.21
fumarate
pH 6.9, 37°C
0.21
fumarate
37°C, pH 6.9
0.28
fumarate
pH 6.9, 37°C
0.28
fumarate
37°C, pH 6.9
0.32
fumarate
-
pH 8, 37°C, Vmax: 1430 micromol/minute/mg/
0.34
fumarate
Q8U062; Q8U063
pH 8, 75°C
0.38
fumarate
MES-NaOH buffer, pH 7.0
0.39
fumarate
-
enzyme form FUMC
0.4
fumarate
pH 7.7, 30°C
0.43
fumarate
-
pH 7.0, 55°C
0.46
fumarate
-
pH 8, 37°C, Vmax: 1900 micromol/minute/mg/
0.5
fumarate
pH 7.7, 30°C
0.5
fumarate
presence of 3 mM oxalacetate, pH 8.0, 30°C
0.5
fumarate
presence of 3 mM oxaloacetate, pH 8.0, 30°C
0.6
fumarate
-
fumarase A
0.67
fumarate
MES-NaOH buffer, pH 7.0
0.7
fumarate
pH 8.0, 30°C
0.81
fumarate
MES-NaOH buffer, pH 6.0
0.9
fumarate
-
pH 6.9, 37°C
0.9
fumarate
37°C, pH 6.9
1.3
fumarate
-
pH 8.7, temperature not specified in the publication, aerobic condition, Vmax: 1.8 micromol/min/mg
1.7
fumarate
-
enzyme form FUMB
1.9
fumarate
-
pH 9, temperature not specified in the publication, aerobic condition, Vmax: 44.3 micromol/min/mg
2.5
fumarate
-
pH 8.7, temperature not specified in the publication, anaerobic condition, Vmax: 26.4 micromol/min/mg
3.07
fumarate
pH 7.4, 30°C, recombinant enzyme
3.1
fumarate
phosphate buffer, pH 6.0
3.8
fumarate
phosphate buffer, pH 7.0
4.2
fumarate
phosphate buffer, pH 6.0
5.7
fumarate
-
pH 9, temperature not specified in the publication, anaerobic condition, Vmax: 186 micromol/min/mg
8.8
fumarate
-
pH 7.4, 37°C
0.0025
L-malate
isoform Fum2, pH 7.5, temperature not specified in the publication
0.0125
L-malate
isoform Fum1, pH 7.5, temperature not specified in the publication
0.049
L-malate
-
enzyme form FUMA
0.05
L-malate
-
enzyme form FUMC
0.156
L-malate
mutant N161E, pH 7.3, 30°C
0.2
L-malate
37°C, pH 6.9
0.216
L-malate
mutant D162W, pH 7.3, 30°C
0.268
L-malate
mutant P160A, pH 7.3, 30°C
0.28
L-malate
pH 6.9, 30°C
0.3
L-malate
-
pH 8, 37°C, Vmax: 490 micromol/minute/mg/
0.35
L-malate
mutant P160T, pH 7.3, 30°C
0.4
L-malate
37°C, pH 6.9
0.42
L-malate
pH 6.9, 30°C
0.5
L-malate
presence of 3 mM oxalacetate, pH 8.0, 30°C
0.559
L-malate
mutant P160H, pH 7.3, 30°C
0.574
L-malate
wild-type, pH 7.3, 30°C
0.6
L-malate
pH 8.2, 30°C
0.6
L-malate
presence of 3 mM oxaloacetate, pH 8.0, 30°C
0.7
L-malate
-
pH 8, 37°C, Vmax: 720 micromol/minute/mg/
0.78
L-malate
37°C, pH 6.9
0.783
L-malate
mutant H159S, pH 7.3, 30°C
0.797
L-malate
mutant N161R, pH 7.3, 30°C
0.835
L-malate
mutant D162M, pH 7.3, 30°C
0.909
L-malate
mutant N161F, pH 7.3, 30°C
0.93
L-malate
37°C, pH 6.9
1.08
L-malate
mutant D162K, pH 7.3, 30°C
1.1
L-malate
mutant A308T, pH 7.4, 23°C
1.267
L-malate
mutant H159V, pH 7.3, 30°C
1.282
L-malate
mutant H159Y, pH 7.3, 30°C
1.8
L-malate
pH 8.0, 30°C
1.9
L-malate
pH 8.2, 30°C
1.9
L-malate
wild-type, pH 7.4, 23°C
2
L-malate
mutant H318Y, pH 7.4, 23°C
2.94
L-malate
-
enzyme form FUMC
6.7
L-malate
-
pH 6.5, 40°C
15
L-malate
-
pH 7.3, 40°C
0.03
mesaconate
pH 8.0, 30°C
0.03
mesaconate
pH 6.9, 30°C
0.1
mesaconate
pH 6.9, 37°C
0.1
mesaconate
37°C, pH 6.9
0.15
mesaconate
-
pH 6.9, 37°C
0.15
mesaconate
37°C, pH 6.9
0.22
mesaconate
pH 6.9, 37°C
0.22
mesaconate
37°C, pH 6.9
0.005
S-malate
-
pH 6.5 cytosolic form, Vmax: 4.5 micromol/min/mg, temperature not specified in the publication
0.05
S-malate
-
pH 7 mitochondrial, Vmax: 0.3 micromol/min/mg, temperature not specified in the publication
1.2
S-malate
-
pH 8.7, temperature not specified in the publication, aerobic condition, Vmax: 0.5 micromol/min/mg
2.3
S-malate
-
pH 8.7, temperature not specified in the publication, anaerobic condition, Vmax: 11.8 micromol/min/mg
5.7
S-malate
-
pH 9, temperature not specified in the publication, aerobic condition, Vmax: 22.7 micromol/min/mg
12.6
S-malate
-
pH 9, temperature not specified in the publication, anaerobic condition, Vmax: 138 micromol/min/mg
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additional information
additional information
-
11.2
(S)-malate
-
fumarase A
25.2
(S)-malate
-
pH 7.0, 55°C
34
(S)-malate
MES-NaOH buffer, pH 6.0
48
(S)-malate
phosphate buffer, pH 6.0
110
(S)-malate
MES-NaOH buffer, pH 7.0
200
(S)-malate
phosphate buffer, pH 7.0
290
(S)-malate
MES-NaOH buffer, pH 7.0
460
(S)-malate
phosphate buffer, pH 6.0
1.9
fumarate
-
pH 8.7, temperature not specified in the publication, aerobic condition
28.3
fumarate
-
pH 8.7, temperature not specified in the publication, anaerobic condition
48.6
fumarate
-
pH 9, temperature not specified in the publication, aerobic condition
51.7
fumarate
-
fumarase A
204.2
fumarate
-
pH 9, temperature not specified in the publication, anaerobic condition
219
fumarate
-
pH 7.0, 55°C
310
fumarate
MES-NaOH buffer, pH 6.0
430
fumarate
MES-NaOH buffer, pH 7.0
510
fumarate
phosphate buffer, pH 6.0
650
fumarate
MES-NaOH buffer, pH 7.0
720
fumarate
phosphate buffer, pH 6.0
730
fumarate
phosphate buffer, pH 7.0
1149
fumarate
pH 7.9, native enzyme
1150
fumarate
pH 7.9, native enzyme
0.007
L-malate
mutant N161E, pH 7.3, 30°C
0.011
L-malate
mutant D162W, pH 7.3, 30°C
0.028
L-malate
mutant P160T, pH 7.3, 30°C
0.029
L-malate
mutant N161F, pH 7.3, 30°C
0.033
L-malate
mutant P160H, pH 7.3, 30°C
0.035
L-malate
mutant P160A, pH 7.3, 30°C
0.04
L-malate
mutant H159S, pH 7.3, 30°C
0.041
L-malate
mutant H318Y, pH 7.4, 23°C
0.045
L-malate
mutant N161R, pH 7.3, 30°C
0.048
L-malate
mutant H159V, pH 7.3, 30°C
0.055
L-malate
mutant D162M, pH 7.3, 30°C
0.055
L-malate
wild-type, pH 7.3, 30°C
0.065
L-malate
mutant D162K, pH 7.3, 30°C
0.098
L-malate
mutant H159Y, pH 7.3, 30°C
0.16
L-malate
mutant A308T, pH 7.4, 23°C
1
L-malate
pH 7.9, mutant enzyme E315Q
65
L-malate
-
pH 6.5, 40°C
150
L-malate
wild-type, pH 7.4, 23°C
267
L-malate
-
pH 7.3, 40°C
620
L-malate
-
pH 8, 40°C
0.55
S-malate
-
pH 8.7, temperature not specified in the publication, aerobic condition
12.9
S-malate
-
pH 8.7, temperature not specified in the publication, anaerobic condition
24.9
S-malate
-
pH 9, temperature not specified in the publication, aerobic condition
151.4
S-malate
-
pH 9, temperature not specified in the publication, anaerobic condition
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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0.05 - 2.13
(2S,3S)-tartrate
0.05 - 2.13
(S,S)-Tartrate
0.05
(2S,3S)-tartrate
-
pH 6.9, 37°C
0.065
(2S,3S)-tartrate
pH 6.9, 37°C
0.635
(2S,3S)-tartrate
pH 6.9, 37°C
2.13
(2S,3S)-tartrate
pH 6.9, 37°C
35
(S)-citramalate
37°C, pH 6.9
35
(S)-citramalate
pH 6.9, 37°C
38
(S)-citramalate
37°C, pH 6.9
38
(S)-citramalate
pH 6.9, 37°C
110
(S)-citramalate
37°C, pH 6.9
110
(S)-citramalate
-
pH 6.9, 37°C
131
(S)-citramalate
pH 8.0, 30°C
131
(S)-citramalate
pH 6.9, 30°C
260
(S)-malate
-
pH 6.9, 37°C
320
(S)-malate
pH 8.0, 30°C
370
(S)-malate
pH 6.9, 37°C
390
(S)-malate
pH 6.9, 37°C
398
(S)-malate
pH 8.0, 30°C
870
(S)-malate
pH 6.9, 37°C
3700
(S)-malate
Q8U062; Q8U063
pH 8, 75°C
0.05
(S,S)-Tartrate
37°C, pH 6.9
0.065
(S,S)-Tartrate
37°C, pH 6.9
0.635
(S,S)-Tartrate
37°C, pH 6.9
2.13
(S,S)-Tartrate
37°C, pH 6.9
3
D-Tartrate
-
pH 8, 37°C
12
D-Tartrate
-
pH 8, 37°C
930
D-Tartrate
Q8U062; Q8U063
pH 8, 75°C
8.5
fumarate
presence of 3 mM oxalacetate, pH 8.0, 30°C
9.7
fumarate
presence of 3 mM oxaloacetate, pH 8.0, 30°C
36.6
fumarate
pH 7.7, 30°C
57.6
fumarate
pH 7.7, 30°C
750
fumarate
37°C, pH 6.9
750
fumarate
-
pH 6.9, 37°C
2200
fumarate
pH 8.0, 30°C
2200
fumarate
pH 6.9, 30°C
2800
fumarate
pH 8.0, 30°C
2800
fumarate
pH 6.9, 30°C
3120
fumarate
37°C, pH 6.9
3120
fumarate
pH 6.9, 37°C
3200
fumarate
Q8U062; Q8U063
pH 8, 75°C
3500
fumarate
37°C, pH 6.9
3500
fumarate
pH 6.9, 37°C
4200
fumarate
-
pH 8, 37°C
4500
fumarate
-
pH 8, 37°C
6600
fumarate
37°C, pH 6.9
6600
fumarate
pH 6.9, 37°C
0.0075
L-malate
mutant H159Y, pH 7.3, 30°C
0.021
L-malate
mutant H318Y, pH 7.4, 23°C
0.0317
L-malate
mutant N161F, pH 7.3, 30°C
0.0367
L-malate
mutant H159V, pH 7.3, 30°C
0.0433
L-malate
mutant N161E, pH 7.3, 30°C
0.05
L-malate
mutant D162W, pH 7.3, 30°C
0.05
L-malate
mutant H159S, pH 7.3, 30°C
0.055
L-malate
mutant N161R, pH 7.3, 30°C
0.0583
L-malate
mutant D162K, pH 7.3, 30°C
0.0583
L-malate
mutant P160H, pH 7.3, 30°C
0.065
L-malate
mutant D162M, pH 7.3, 30°C
0.08
L-malate
mutant P160T, pH 7.3, 30°C
0.0967
L-malate
wild-type, pH 7.3, 30°C
0.1283
L-malate
mutant P160A, pH 7.3, 30°C
0.15
L-malate
mutant A308T, pH 7.4, 23°C
8.5
L-malate
pH 8.0, 30°C
8.7
L-malate
pH 8.2, 30°C
9.7
L-malate
-
pH 6.5, 40°C
10.88
L-malate
-
pH 8, 40°C
17.8
L-malate
-
pH 7.3, 40°C
37
L-malate
presence of 3 mM oxalacetate, pH 8.0, 30°C
37.8
L-malate
presence of 3 mM oxaloacetate, pH 8.0, 30°C
80
L-malate
wild-type, pH 7.4, 23°C
260
L-malate
37°C, pH 6.9
320
L-malate
pH 6.9, 30°C
370
L-malate
37°C, pH 6.9
390
L-malate
37°C, pH 6.9
398
L-malate
pH 6.9, 30°C
870
L-malate
37°C, pH 6.9
1000
L-malate
-
pH 8, 37°C/
1600
L-malate
-
pH 8, 37°C
250
mesaconate
37°C, pH 6.9
250
mesaconate
pH 6.9, 37°C
580
mesaconate
37°C, pH 6.9
580
mesaconate
pH 6.9, 37°C
2000
mesaconate
37°C, pH 6.9
2000
mesaconate
-
pH 6.9, 37°C
3600
mesaconate
pH 8.0, 30°C
3600
mesaconate
pH 6.9, 30°C
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-
brenda
-
in thin sections from kidney, liver, heart, adrenal gland and anterior pituitary, strong and specific labeling due to fumarase antibody is only detected in mitochondria. In pancreatic acinar cells, in addition to mitochondria, highly significant labeling is also observed in the zymogen granules and endoplasmic reticulum
brenda
-
-
brenda
-
in thin sections from kidney, liver, heart, adrenal gland and anterior pituitary, strong and specific labeling due to fumarase antibody is only detected in mitochondria. In pancreatic acinar cells, in addition to mitochondria, highly significant labeling is also observed in the zymogen granules and endoplasmic reticulum
brenda
additional information
-
enzyme colocalizes with the bacterial DNA
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
about 25% of total activity
brenda
-
-
brenda
-
under normal conditions
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
mitochondrial and cytosolic isoforms are derivatives of a single translation product and have identical amino termini
brenda
-
translation product of the FUM1 gene, distribution can be affected by hsp70 molecular chaperones
brenda
-
the cytosolic isoenzyme and the mitochondrial isoenzyme are identical over nearly all of their amino acid sequences but differ at their N-termini
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
about 75% of total activity
brenda
-
-
brenda
-
brenda
-
-
brenda
Cos-1 cells transfected with fumarase constructs, human fumarase with either the native or cytochrome c oxidase subunit VIII mitochondrial targeting sequence is detected exclusively in mitochondria in more than 98% of the cells, while the remainder 1-2% of the cells shows varying amounts of nuclear labeling. When human fumarase is fused to the yeast mitochondrial targeting sequence, more than 50% of the cells show nuclear labeling
brenda
-
under normal conditions
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
cytosolic fumarase and mitochondrial fumarase are identical products of the same nuclear gene
brenda
-
in thin sections from kidney, liver, heart, adrenal gland and anterior pituitary, strong and specific labeling due to fumarase antibody is only detected in mitochondria. In pancreatic acinar cells, in addition to mitochondria, highly significant labeling is also observed in the zymogen granules and endoplasmic reticulum
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
mitochondrial and cytosolic isoforms are derivatives of a single translation product and have identical amino termini
brenda
-
translation product of the FUM1 gene, distribution can be affected by hsp70 molecular chaperones
brenda
-
the presequence of fumarase is exposed to the cytosol during import into mitochondria
brenda
-
-
brenda
-
-
brenda
-
the cytosolic isoenzyme and the mitochondrial isoenzyme are identical over nearly all of their amino acid sequences but differ at their N-termini
brenda
-
-
brenda
Cos-1 cells transfected with fumarase constructs, human fumarase with either the native or cytochrome c oxidase subunit VIII mitochondrial targeting sequence is detected exclusively in mitochondria in more than 98% of the cells, while the remainder 1-2% of the cells shows varying amounts of nuclear labeling. When human fumarase is fused to the yeast mitochondrial targeting sequence, more than 50% of the cells show nuclear labeling
brenda
-
after both hydroxyurea or ionizing radiation treatments, is localized in the nucleus after DNA damage
brenda
-
is localized in the nucleus after DNA damage
brenda
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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
malfunction
-
in the absence of cytosolic fumarate hydratase, the cellular response to DNA damage is impaired
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
malfunction
isolation of homozygous fum1 knock-out plants from self-fertilized heterozygotes is failing
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
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
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
-
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
-
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
-
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
-
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
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
-
fumarase in permeabilized non-growing cells used as biocatalysts for continuous production of L-malic acid
physiological function
-
fumarase in permeabilized non-growing cells used as biocatalysts for continuous production of L-malic acid
physiological function
-
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
-
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
-
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
-
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
-
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 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
-
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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135000
gel filtration, mutants H318Y and A308T
160000
-
sucrose density gradient centrifugation
194000
-
equilibrium sedimentation
210000
gel filtration, wild-type
440000
-
oligomer 1, gel filtration
46000
-
4 * 46000, SDS-PAGE
47900
calculated from amino acid sequence
48500
-
4 * 48500, equilibrium sedimentation in 6 M guanidine HCl, pH 4.25
50502
x * 50502, calculation from nucleotide sequence
50900
-
x * 50900, about, sequence calculation, x * 43000-45000, recombinant enzyme, SDS-PAGE
51000
x * 51000, SDS-PAGE
54000
-
mitochondrial fumarate hydratase is translated as an approximately 54000 Da precursor, which is processed upon mitochondrial transport by cleavage of the N-terminal targeting signal, resulting in a mature form of 48000 Da
600000
-
oligomer 2, gel filtration
61000
-
2 * 61000, enzyme form FUMA, SDS-PAGE
61100
-
calculated from cDNA
62600
-
calculated from cDNA
120000
-
gel filtration
120000
-
enzyme form FUMA, gel filtration
180000
-
-
195000
gel filtration
195000
-
calculation from amino acid analysis
200000
gel filtration
200000
-
sucrose density gradient centrifugation
200000
-
enzyme form FUMC, gel filtration
200000
-
Fe-S-independent enzyme form, gel filtration
45000
SDS-PAGE
45000
-
4 * 45000, SDS-PAGE
48000
-
mitochondrial fumarate hydratase is translated as an approximately 54000 Da precursor, which is processed upon mitochondrial transport by cleavage of the N-terminal targeting signal, resulting in a mature form of 48000 Da
48000
-
4 * 48000, Fe-S-independent enzyme form, SDS-PAGE
49000
-
SDS-PAGE
49000
-
4 * 49000, SDS-PAGE in presence of 8 M urea
50000
SDS-PAGE
50000
-
4 * 50000, SDS-PAGE
50000
-
4 * 50000, SDS-PAGE
50000
4 * 50000, SDS-PAGE
50000
-
4 * 50000, enzyme form FUMC, SDS-PAGE
60000
SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
60000
-
2 * 60000, enzyme form FUMA, SDS-PAGE
60105
calculated from sequence
60105
-
calculated from sequence
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A227V
3.3-fold improvement of half-life at 50°C and a 3.6°C increase in temperature at which the activity of enzyme decreases by 50% in 15 min compared to the wild-type enzyme
A227V/A411V
half-life at 50°C and temperature at which the activity of enzyme decreases by 50% in 15 min increases to more than 768 min and 52.4°C, respectively
A227V/A411V/E175K
half-life at 50°C increases to more than 2700 min and the temperature at which the activity of enzyme decreases by 50% in 15 min is 9.8°C higher than the wild-type enzyme
A411V
half-life at 50°C increases from 1 min for wild-type to 2.2 min, and the temperature at which the activity of enzyme decreases by 50% in 15 min increases from 44.8°C to 47.2°C
A227V
-
3.3-fold improvement of half-life at 50°C and a 3.6°C increase in temperature at which the activity of enzyme decreases by 50% in 15 min compared to the wild-type enzyme
-
A227V/A411V
-
half-life at 50°C and temperature at which the activity of enzyme decreases by 50% in 15 min increases to more than 768 min and 52.4°C, respectively
-
A227V/A411V/E175K
-
half-life at 50°C increases to more than 2700 min and the temperature at which the activity of enzyme decreases by 50% in 15 min is 9.8°C higher than the wild-type enzyme
-
A411V
-
half-life at 50°C increases from 1 min for wild-type to 2.2 min, and the temperature at which the activity of enzyme decreases by 50% in 15 min increases from 44.8°C to 47.2°C
-
E315Q
mutation causes about 3% increase in Km-value for S-malate, about 20% increase in Km-value for fumarate. 10fold decrease in turnover number for S-malate, about 11fold decrease in turnover number for fumarate
H129N
-
loss of D2O inhibitory effect, product release step is accelerated by glycerol compared to inhibition of wild-type enzyme. 3.1fold reduced maximal velococity in reaction with malate, 1.13fold reduced maximal velocity in reaction with fumarate compared to wild-type enzyme
K127D
-
mutant enzyme behaves like wild-type enzyme
R126A
-
loss of D2O inhibitory effect, product release step is accelerated by glycerol compared to inhibition of wild-type enzyme. 4.3fold reduced maximal velococity in reaction with malate, 2.7fold reduced maximal velocity in reaction with fumarate compared to wild-type enzyme
R126A/H129N
-
great loss of D2O inhibitory effect, product release step is accelerated by glycerol compared to inhibition of wild-type enzyme. 8.6fold reduced maximal velococity in reaction with malate, 7.1fold reduced maximal velocity in reaction with fumarate compared to wild-type enzyme
H129N
-
loss of D2O inhibitory effect, product release step is accelerated by glycerol compared to inhibition of wild-type enzyme. 3.1fold reduced maximal velococity in reaction with malate, 1.13fold reduced maximal velocity in reaction with fumarate compared to wild-type enzyme
-
K127D
-
mutant enzyme behaves like wild-type enzyme
-
R126A
-
loss of D2O inhibitory effect, product release step is accelerated by glycerol compared to inhibition of wild-type enzyme. 4.3fold reduced maximal velococity in reaction with malate, 2.7fold reduced maximal velocity in reaction with fumarate compared to wild-type enzyme
-
R126A/H129N
-
great loss of D2O inhibitory effect, product release step is accelerated by glycerol compared to inhibition of wild-type enzyme. 8.6fold reduced maximal velococity in reaction with malate, 7.1fold reduced maximal velocity in reaction with fumarate compared to wild-type enzyme
-
A117P
-
missense mutation
A239T
-
missense mutation
A274T
-
missense mutation
A308T
mutation associated with fumarate hydratase deficiency and hereditary leiomyomatosis and renal cell cancer. Enzyme shows severely diminished fumarase activity, and the variant is largely defective due to decreased turnover rate, while displaying Km values for L-malate similar to wild-type. The protein forms homodimers rather than homotetramers
A308Y
-
the mutation is associated with fumarase deficiency
A385D
-
missense mutation
C333Y
-
missense mutation
D425V
-
the mutation is associated with fumarase deficiency
E319Q
-
mutant with strongly reduced activity
E355K
-
missense mutation
E362Q
-
the mutation is associated with fumarase deficiency
F312C
-
the mutation is associated with fumarase deficiency
G282V
-
missense mutation
G397R
-
missense mutation
H135R
-
missense mutation
H180R
-
missense mutation
H318L
-
the mutation is associated with fumarase deficiency
H318Y
mutation associated with fumarate hydratase deficiency and hereditary leiomyomatosis and renal cell cancer. Enzyme shows severely diminished fumarase activity, and the variant is largely defective due to decreased turnover rate, while displaying Km values for L-malate similar to wild-type. The protein forms homodimers rather than homotetramers
H402C
-
the mutation is associated with fumarase deficiency
I229T
-
missense mutation
I77V
-
the mutant enzyme shows increased activity
K230R
-
missense mutation
K467R
-
missense mutation
L335P
-
missense mutation
L507P
-
missense mutation
M195T
-
missense mutation
M368T
-
the mutation is associated with hereditarymultiplecutaneous leiomyoma
M454I
-
missense mutation
N107T
-
missense mutation
N188S
-
missense mutation
N310Y
-
missense mutation
N330S
-
missense mutation detected in a patient with a bilateral renal cell cancer
N340K
-
missense mutation
N362K
-
the mutation is associated with renal cell cancer
P174R
-
missense mutation
P192L
-
missense mutation
P369S
-
the mutation is associated with fumarase deficiency
Q142K
-
missense mutation
Q185R
-
missense mutation
Q376P
-
the mutation is associated with fumarase deficiency
Q439P
-
the mutation is associated with renal cell cancer
R101P
-
the mutation is associated with renal cell cancer
R101X
-
the mutation is associated with renal cell cancer
R160G
-
missense mutation
R233C
-
the mutation is associated with renal cell cancer
R233H
-
the mutation is associated with renal cell cancer
R233L
-
the mutation is associated with renal cell cancer
R343X
-
the mutation is associated with renal cell cancer
S158I
-
missense mutation
S187L
-
missense mutation
S334R
-
the mutation is associated with hereditarymultiplecutaneous leiomyoma
S365G
-
missense mutation
S365N
-
missense mutation
S41P
-
the mutation is associated with renal cell cancer
T330P
-
missense mutation
V322D
-
missense mutation
V394L
-
missense mutation
Y465C
-
missense mutation
S318A
mutant shows no activity
S318C
mutant shows no activity
S318A
-
mutant shows no activity
-
S318C
-
mutant shows no activity
-
K481E
the activity of fumarase is lower in Dahl salt-sensitive SS rats compared with SS.13BN rats. SS.13BN rats have a Brown Norway (BN) allele of fumarase and exhibit attenuated hypertension. The SS allele of fumarase differs from the BN allele by a K481E sequence variation
D162K
increase in Km, decrease in kcat/Km value
D162M
increase in Km, decrease in kcat/Km value
D162W
decrease in Km and kcat/Km value
H159S
increase in Km, decrease in kcat/Km value
H159V
increase in Km, decrease in kcat/Km value
H159Y
increase in Km, decrease in kcat/Km value
N161E
decrease in Km and kcat/Km value
N161F
increase in Km, decrease in kcat/Km value
N161R
increase in Km, decrease in kcat/Km value
P160A
decrease in Km value, kcat/Km increases by 33.2%
P160H
decrease in Km and kcat/Km value
P160T
decrease in Km and kcat/Km value
H159Y
-
increase in Km, decrease in kcat/Km value
-
N161E
-
decrease in Km and kcat/Km value
-
P160A
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decrease in Km value, kcat/Km increases by 33.2%
-
P160H
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decrease in Km and kcat/Km value
-
P160T
-
decrease in Km and kcat/Km value
-
H153R
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is catalytically inactive since it does not complement a fumarase knockout strain with respect to its TCA cycle function. Yeast strains expressing the mutant protein do not grow on glycerol as the sole energy and carbon source
A347S
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mutation results in an increase in optimum temperature of 10°C and a fourfold enhancement in specific activity
G163R
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mutation results in an increase in optimum temperature of 5°C
G163R/G170E
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mutant is more thermostable than wild-type scFUMC. Mutation results in an increase in optimum temperature of 5°C
G163R/G170E/A347S
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mutant is more thermostable than wild-type scFUMC. Mutation results in an increase in optimum temperature of 5°C
G170E
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mutation results in an increase in optimum temperature of 5°C
G170E/A347S
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mutation results in an increase in optimum temperature of 5°C
K424R
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missense mutation
K424R
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the activity of the mutated protein is significantly reduced as compared to wild type
R190H
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almost inactive mutant, the R190H missense mutation is the most frequent in hereditary leiomyomatosis and renal cell cancer patients
R190H
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the mutation is associated with renal cell cancer
additional information
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E319Q mutation, an inborn error of fumarase causes progressive psychomotor retardation, failure to thrive, microcephaly and abnormal posture with hypotonia contrasting with hypertonia of limbs
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
additional information
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isolation of fumarase mutants in which dual targeting (to cytosol and mitochondria) is abolished because of perturbation of its conformation
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100
-
30 min, complete loss of activity
15 - 70
-
30 min, pH 8.5, activity of FumF is stable with increasing temperature below 58°C in the absence of any stabilizer. When the temperature is higher than 60°C, FumF protein loses almost 50% of its activity
20
-
half-life: 1.6 h, at 0.0438 mg of protein per ml
4
-
half-life: 4.6 h, at 0.0438 mg of protein per ml
44.8
wild-type, 15 min, 50% residual activity
45
purified recombinant enzyme, stable below
47.2
mutant A411V, 15 min, 50% residual activity
49
-
5 min, 50% inhibition, enzyme form FUMA
49.4
mutant A227V, 15 min, 50% residual activity
51
-
5 min, 50% inhibition, enzyme form FUMA
52.4
mutant A227V/A411V, 15 min, 50% residual activity
54.6
mutant A227V/A411V/E175K, 15 min, 50% residual activity
56.3
-
melting temperature
57.7
-
melting temperature
75
-
24 h, 10% loss of activity
40
-
over 85% of activity after 48 h incubation at 40°C
50
half-life of wild-type 1 min, of mutant A411V 2.2 min, of mutant A227V 4.3 min, of mutant A227V/A411V more than 768 min, of mutant A227V/A411V/E175K more than 2700 min
50
-
80 min, 30% loss of activity of the enzyme form FUMC. Rapid inactivation of enzyme form FUMA and FUMB
50
-
complete inactivation within several seconds
50
-
rapid denaturation at
70
-
1 h, stable
70
30 min, no significant loss of activity
90
-
30 min, 72% of maximal activity
90
-
30 min, 72% loss of activity
90
-
24 h, 20% loss of activity
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(NH4)2SO4, protects enzyme form FUMA from inactivation at 4°C
-
0.8 M guanidine hydrochloride, 50% loss of activity after 5 min at 75°C, complete inactivation at concentrations above 1.5 M
-
10% glycerol, 0.1 M KCl, 5 mM L-malate or 30% ethyleneglycol, partially protects enzyme form FUMA from inactivation at 4°C
-
50% v/v ethanol, 50% v/v methanol, 50% v/v 2-propanol, 4 M urea or 0.1% SDS, stable after treatment for 10 h at room temperature
-
dithiothreitol partially restores from urea and alkaline inactivation
enzyme form FUMA, oxidation and the concomitant release of iron inactivates the enzyme in a reversible manner
-
enzyme form FUMB is extremely unstable
-
enzyme stability is achieved by addition of soy bean protein or bovine serum albumin.
-
exposure to air at room temperature causes 50% loss of activity, reactivation with FeSO4 and 2-mercaptoethanol
-
exposure to air results in 30% decreased activity
-
mitochondrially targeted fumarase harboring a tobacco etch virus protease recognition sequence is efficiently cleaved by the mitochondrial but not by the cytosolic tobacco etch virus protease. Fumarase is readily cleaved by cytosolic tobacco etch virus when its import into mitochondria is slowed down by either disrupting the activity of the TOMcomplex, lowering the growth temperature, or reducing the inner membrane electrochemical potential
-
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Ethylene glycol
in presence of 70 % ethylene glycol, about 47 % L-malic acid is converted to fumaric acid, at 50 % ethylene glycol 38 % conversion occurs and at 30 % ethylene glycol 32 % conversion, respectively. After 2 days, no significant loss of activity in 50 % ethylene glycol is observed, in 70 % ethylene glycol, 80 % activity of the fumarase remain
2-propanol
-
50% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
2-propanol
-
50% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
-
Ethanol
-
50% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
Ethanol
-
50% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
-
Methanol
-
50% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
Methanol
-
50% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
-
SDS
-
0.1% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
SDS
-
0.1% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
-
urea
-
0.1% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
urea
-
0.1% (v/v), 10 h at room temperature, no significant loss of activity, slight loss of activity after 14 days
-
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a pfl ldhA double mutant Escherichia coli strain NZN11 is used to produce succinic acid by overexpressing the Escherichia coli malic enzyme gene sfcA. This strain, however, produces a large amount of malic acid as well as succinic acid. The fumB gene encoding the anaerobic fumarase of Escherichia coli is co-amplified to solve the problem of malic acid accumulation, and subsequently improve the succinic acid production
-
Cos-1 cells transfected with fumarase constructs, human fumarase with either the native or cytochrome c oxidase subunit VIII mitochondrial targeting sequence is detected exclusively in mitochondria in more than 98% of the cells, while the remainder 1-2% of the cells shows varying amounts of nuclear labeling. When human fumarase is fused to the yeast mitochondrial targeting sequence, more than 50% of the cells show nuclear labeling
entire protein-coding region of fumarase cDNA cloned from Dahl salt-sensitive, SS-13BN, and Brown Norway rats. PCR product inserted into the T-easy vector and propagated in competent Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as His-tagged fusion proteins
-
expressed in Escherichia coli strain JM109
expressed in HK-2 cells and in skin fibroblasts
-
expressed in yeast FUM1 mutant strain
-
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli lysY
expression in Escherichia coli mutant EJ1535
-
FUM1-green fluorescent protein (GFP) expressed driven by the 35S promoter in Arabidopsis thaliana cell cultures
FUM2-red fluorescent protein (RFP) fusions epressed by the 35S promoter, introduced into Arabidopsis thaliana cell cultures
gene fumF, cloned from a plasmid metagenomic library, DNA and amino acid sequence determination and analysis, sequence comparison, and phylogenetic analysis
-
gene fumR, overexpression in Escherichia coli strain BL21 (DE3)
gene HP1325, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
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mutant fumarase derivative lacking the MTS expressed in the FUM1 mutant strain, expressing the site-specific HO double-stranded DNA endonuclease
-
overexpression in Escherichia coli
Q8U062; Q8U063
plasmid encoding fumarase lacking an MTS transformed into the wild-type, DELTAcit2 and R strains
-
-
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21
expression in Escherichia coli lysY
expression in Escherichia coli lysY
expression in Escherichia coli lysY
-
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at least 15fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
expression is induced by growth on acetate and mesaconate
expression is induced upon DNA damage
-
fumarate hydratase levels increase 2fold after 24 h of treatment with double-strand breaks. Is overexpressed in response to DNA damage
-
is overexpressed in response to DNA damage
-
knock down of total cellular fumarate hydratase expression using specific shRNA
-
level of FUM2 RNA in rosette leaves is higher in the light than in the dark, but total fumarase activity remains constant throughout the diurnal cycle
level of fumarase mRNA is upregulated both in the DELTacit2 and wild-type plus pCit2 strains. Approximately 2fold higher Fum1 mRNA level in a DELTAcit2 strain when compared with the wild-type strain. Significant increase in fumarase expression and cellular enzymatic activity in the glyoxylate deletion strains: DELTAmls1, DELTAicl1, DELTAaco1and DELTAcit2. Succinic acid in the growth medium affects fumarase dual distribution, succinic acid directly interacts with fumarase and slows down its folding thereby causing more fumarase to be fully imported into mitochondria
-
the expression of the Fum2 gene is unaffected by phytochrome both in darkness and in light
the main regulator of Fum1 gene transcription, is phytochrome A. The active form of phytochrome A suppresses Fum1 expression. The signal transduction mechanism operates via Ca2+ activation of expression of the gene encoding the transcription factor PIF3, which binds to promoters of phytochrome-regulated genes and inhibits Fum1 expression
at least 15fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
at least 15fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
-
-
expression is induced by growth on acetate and mesaconate
expression is induced by growth on acetate and mesaconate
-
-
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analysis
-
fumarate hydratase activity can be useful in the diagnosis of hereditary leiomyomatosis and renal cell cancer in cases with atypical presentation and undetectable fumarate hydratase mutations. Furthermore, fumarate hydratase activity testing is of value in laboratory investigations to elucidate the mechanism of hereditary leiomyomatosis and renal cell cancer
industry
-
use of purified enzyme in L-malic acid production is uneconomical because whole cells are cheaper. Use of one mg of purified fumarase in continuous production of L-malic acids, corresponds to the use of enzyme in 68 g (wet weight) cells of Saccharomyces bayanus or in 120 g (wet weight) cells of baker's yeast
industry
-
use of purified enzyme in L-malic acid production is uneconomical because whole cells are cheaper. Use of one mg of purified fumarase in continuous production of L-malic acids, corresponds to the use of enzyme in 68 g (wet weight) cells of Saccharomyces bayanus or in 120 g (wet weight) cells of baker's yeast
industry
-
use of purified enzyme in L-malic acid production is uneconomical because whole cells are cheaper. Use of one mg of purified fumarase in continuous production of L-malic acids, corresponds to the use of enzyme in 68 g (wet weight) cells of Saccharomyces bayanus or in 120 g (wet weight) cells of baker's yeast
medicine
-
metabolites of ibuprofen may play a role in its anti-cataract effect by protecting lenticular enzymes
medicine
-
fumarate hydratase activity can be useful in the diagnosis of hereditary leiomyomatosis and renal cell cancer in cases with atypical presentation and undetectable fumarate hydratase mutations. Furthermore, fumarate hydratase activity testing is of value in laboratory investigations to elucidate the mechanism of hereditary leiomyomatosis and renal cell cancer
medicine
-
fumarate immunohistochemistry may serve as a useful low-cost screening method to identify hereditary leiomyomatosis and renal cancer
medicine
-
whole-gene fumarate hydratase deletions are not a frequent cause of hereditary leiomyomatosis and renal cell cancer syndrome
medicine
elevation of total fumarase activity may attenuate the development of hypertension
medicine
-
the degradation of cell membranes in connection with necrosis leads to elevated fumarase activity in plasma and urine and hyperpolarized [1,4-13C2]malate production 24 h after reperfusion correlates with renal necrosis in a 40-min unilateral ischemic rat model. Fumarase activity screening on bio-fluids can detect injury severity. After verification of renal injury by bio-fluid analysis the precise injury location can be monitored by in vivo measurements of the fumarase activity non-invasively by hyperpolarized [1,4-13C]fumarate magnetic resonance imaging
synthesis
-
highly stable enzyme would be ideal for use in various industrial processes, especially since the specific activity is also very high
synthesis
-
economic production of L-malate in an enzyme membrane reactor
synthesis
-
production of (S)-malic acid, which is used as an acidurant in fruit and vegetable juices, carbonated soft drinks, jams and candies, in amino acid infusions and for the treatment of hepatic malfunctioning
synthesis
-
a pfl ldhA double mutant Escherichia coli strain NZN11 is used to produce succinic acid by overexpressing the Escherichia coli malic enzyme gene sfcA. This strain, however, produces a large amount of malic acid as well as succinic acid. The fumB gene encoding the anaerobic fumarase of Escherichia coli is co-amplified to solve the problem of malic acid accumulation, and subsequently improve the succinic acid production
synthesis
stFUMC is a highly efficient, thermostable fumarase C with industrial potential
synthesis
-
fumarase is used for the industrial production of L-malate from the substrate fumarate
synthesis
overexpression of mutant P160A in Torulopsis glabrata leads to production 5.2 g/l fumarate. Additional deletion of adenylosuccinate synthase, a component of the purine nucleotide cycle, results in production of 9.2 g/l fumarate
synthesis
synthesis of fumarate in 50% ethylene glycol to shift the reaction equilibrium to fumaric acid. 54.7% conversion is observed using fumarase for transforming 1 mmol L-malic acid. 27% total yield is obtained with 99% purity
synthesis
use of tryptophan synthase in the generation of L-dihalotryptophans and L-alkynyltryptophans
synthesis
use of tryptophan synthase in the generation of L-dihalotryptophans and L-alkynyltryptophans
synthesis
-
use of tryptophan synthase in the generation of L-dihalotryptophans and L-alkynyltryptophans
-
synthesis
-
overexpression of mutant P160A in Torulopsis glabrata leads to production 5.2 g/l fumarate. Additional deletion of adenylosuccinate synthase, a component of the purine nucleotide cycle, results in production of 9.2 g/l fumarate
-
synthesis
-
use of tryptophan synthase in the generation of L-dihalotryptophans and L-alkynyltryptophans
-