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10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
10-formyl-5,8-dideazafolate tetraglutamate + NADP+ + H2O
5,8-dideazafolate tetraglutamate + CO2 + NADPH + H+
-
-
tightly bound product
ir
10-formyltetrahydrofolate + NADP+ + H2O
?
the enzyme is composed of three domains and possesses three catalytic activities but has only two catalytic centers. The amino-terminal domain (residues 1-310) bears 10-formyltetrahydrofolate hydrolase activity, the carboxyl-terminal domain (residues 420-902) bears an aldehyde dehydrogenase activity, and the full-length FDH produces 10-formyltetrahydrofolate dehydrogenase activity
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-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O
tetrahydropteroylhexaglutamate + CO2 + NADPH
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
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-
-
-
?
additional information
?
-
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
-
-
?
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
good substrate
-
ir
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
-
-
?
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
-
-
?
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
-
-
?
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
good substrate
-
?
10-formyl-5,8-dideazafolate + NADP+ + H2O
5,8-dideazafolate + CO2 + NADPH + H+
-
stable synthetic analogue can substitute for the labile natural substrate, affinity is twice as high as for 10-formyltetrahydrofolate
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
Cys-707 is involved in enzyme activity
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
enzyme is an important factor in regulation of formate oxidation and is related with methanol poisoning
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
folate-dependent metabolism of formate to carbon dioxide
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate and of the purine biosynthesis through control of the level of 10-formyltetrahydrofolate, down-regulation of FDH in tumors is one of the cellular mechanisms that enhance proliferation, FDH possesses tumor specific suppressor effects
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
folate-dependent pathway is the exclusive route of formate metabolism in primates, plays major role in disposition of formate generated from one-carbon moieties of environmental chemicals, drugs, and foods, importance in the toxicity of methanol
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
a major liver enzyme, contributing to more than one metabolic pathway, regeneration of the tetrahydrofolate pool, not essential for viability
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
ir
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
structure of enzyme domains and of catalytic centers
high affinity for tetrahydrofolate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
enzyme requires Cys-707 to form a thiohemiacetal with the formyl group of 10-formyltetrahydrofolate
high affinity for tetrahydrofolate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
enzyme binds one molecule of tetrahydrofolate and two molecules of NADP+ per tetramer, tetrahydrofolate and NADP+ bind to separate domains, higher affinity for NADP+ at lower enzyme concentrations
high affinity for tetrahydrofolate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate in the cell in response to yet unknown aldehyde and thiol metabolites
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
very tight binding of product, binds its product rather than its substrate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
natural substrate
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
Asp-142 is an essential residue in enzyme mechanism, it influences folate binding, model of substrate binding pocket
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
His-106 is involved in enzyme catalysis and in folding of the N-terminal domain, enzyme requires Cys-707 for catalysis, which is located inside the C-terminal domain, mechanism includes hydrolase reaction as essential part
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
structure of enzyme domains and of catalytic centers
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
Cys-707 is a key residue of the dehydrogenase active site and acts as nucleophile in the formation of an enzyme-linked thiohemiacetal intermediate
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
10-formyltetrahydrofolate is associated with enzyme when it is rapidly isolated, after storage for 24 h before separation of the binding proteins there remains none and tetrahydrofolate is the predominant form bound to enzyme because of the hydrolase activity
very tight binding of product, binds its product rather than its substrate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
mechanism which proceeds through thiohemiacetal and thioester intermediates, nucleophilic attack by the essential active site Cys-707 on the carbonyl group of 10-formyltetrahydrofolate, folate binding domain requires presence of an intact ring system
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
recycling of excess 10-formyltetrahydrofolate that is not needed for purine biosynthesis and restoration of the tetrahydrofolate pool, important for formate metabolism by clearing it as CO2 and thus protecting cells from formate intoxication
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
regulatory mechanism to control the in vivo folate pool size
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
disposal of excess one-carbon units, oxidation of one-carbon moieties is regulated by the ratio of formyltetrahydrofolate to tetrahydrofolate in liver, regulation of the proportion of folate present in the tetrahydrofolate form, presumably to make it available for other reactions of one-carbon metabolism
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
folate-dependent metabolism of formate to carbon dioxide
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
a major folate-binding protein of liver cytosol, 10-formyltetrahydrofolate polyglutamates are tightly bound in vivo
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
very tight binding of product, binds its product rather than its substrate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
very tight binding of product, binds its product rather than its substrate
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
specific for NADP+
-
ir
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
calculated equilibrium constant: 160000000, specific for (-)-10-formyltetrahydrofolate and NADP+
-
ir
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
disposal of excess one-carbon units, oxidation of one-carbon moieties is regulated by the ratio of formyltetrahydrofolate to tetrahydrofolate in liver, regulation of the proportion of folate present in the tetrahydrofolate form, presumably to make it available for other reactions of one-carbon metabolism
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
major disposal route for excess one-carbon units produced in folate-mediated metabolism
-
?
10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O
tetrahydropteroylhexaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O
tetrahydropteroylhexaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
product binds 60fold more tightly than the substrate
-
ir
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
important site of binding of folylpolyglutamates in liver, regulation of the interconversion of 10-formyltetrahydropteroylpolyglutamate to tetrahydropteroylpolyglutamate and therefore of the high-energy formyl charge of the cell
-
ir
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
natural substrate
-
?
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
-
-
-
ir
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
-
-
-
-
?
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
-
affinity increases with increasing length of polyglutamyl chain
-
-
?
additional information
?
-
enzyme does not catalyze the oxidation of 10-formyltetrahydrofolate or propanal
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-
?
additional information
?
-
-
enzyme does not catalyze the oxidation of 10-formyltetrahydrofolate or propanal
-
-
?
additional information
?
-
-
FDH-expressing cells show accumulation of cells in G0-G1 phase and a sharp decrease of cells in S phase. Accumulation of the tumor suppressor protein p53 and its downstream target p21. FDH antiproliferative effects on A549 cells include both G1 cell cycle arrest and caspase-dependent apoptosis
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-
?
additional information
?
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-
activation of p53 tumor suppressor protein-dependent pathways is a general downstream mechanism in response to induction of enzyme expression in p53 functional cancer cells
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-
?
additional information
?
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-
enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate
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-
?
additional information
?
-
-
enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate
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-
?
additional information
?
-
-
enzyme consists of two independent folded domains connected by a linker sequence: a 32 kDa N-terminal domain with 10-formyltetrahydrofolate binding site shows hydrolase activity and a 63 kDa C-terminal domain with NADP+ binding site and Cys-707 shows aldehyde dehydrogenase activity, native structure of enzyme is necessary for 10-formyltetrahydrofolate dehydrogenase activity
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?
additional information
?
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-
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-
?
additional information
?
-
-
enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate
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-
?
additional information
?
-
-
enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate
-
-
?
additional information
?
-
-
enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate
-
-
?
additional information
?
-
-
enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate
-
-
?
additional information
?
-
-
hydrolysis at 25% of dehydrogenase activity
-
-
?
additional information
?
-
-
10-formyltetrahydrofolate dehydrogenase/hydrolase activities occur at the same time and are associated with separate active sites
-
-
?
additional information
?
-
-
10-formyltetrahydrofolate dehydrogenase/hydrolase activities occur at the same time and are associated with separate active sites
-
-
?
additional information
?
-
-
enzyme catalyzes also NADP+-independent hydrolytic cleavage of 10-formyltetrahydrofolate to tetrahydrofolate and formate, hydrolysis is very inefficient compared to dehydrogenase reaction and may be an artifact of assay system
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-
?
additional information
?
-
-
bifunctional enzyme: NADP+-dependent dehydrogenase activity and NADP+-independent hydrolase activity of 10-formyltetrahydrofolate with two active sites
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-
?
additional information
?
-
-
10-formyltetrahydrofolate dehydrogenase and hydrolase are closely related and separately compartmentalized enzymes
-
-
?
additional information
?
-
-
2fold higher 10-formyltetrahydrofolate dehydrogenase than hydrolase activity, hydrolase and dehydrogenase catalytic centers are overlapping
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-
?
additional information
?
-
-
irreversible covalent linkage of 5-formyltetrahydrofolate to enzyme, 2 mol bound per mol of enzyme monomer, 5-formyltetrahydrofolate is not the natural substrate and arises from 10-formyltetrahydrofolate
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-
?
additional information
?
-
-
310 amino acid residue N-terminal domain has 10-formyltetrahydrofolate hydrolase activity and substrate binding site, C-terminal domain has aldehyde dehydrogenase activity and is used as catalytic center in dehydrogenase reaction, full-length enzyme is required for 10-formyltetrahydrofolate dehydrogenase activity, the two domains work in concert
-
-
?
additional information
?
-
-
310 amino acid residue N-terminal domain has 10-formyltetrahydrofolate hydrolase activity and substrate binding site, C-terminal domain has aldehyde dehydrogenase activity and is used as catalytic center in dehydrogenase reaction, full-length enzyme is required for 10-formyltetrahydrofolate dehydrogenase activity, the two domains work in concert
-
-
?
additional information
?
-
-
310 amino acid residue N-terminal domain has 10-formyltetrahydrofolate hydrolase activity and substrate binding site, C-terminal domain has aldehyde dehydrogenase activity and is used as catalytic center in dehydrogenase reaction, full-length enzyme is required for 10-formyltetrahydrofolate dehydrogenase activity, the two domains work in concert
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-
?
additional information
?
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-
FDH has also methyltransferase activity
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-
?
additional information
?
-
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bifunctional protein: 10-formyltetrahydrofolate dehydrogenase/hydrolase, hydrolysis at 20-30% of the oxidative rate
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-
?
additional information
?
-
-
hydrolysis catalyzed by enzyme at 21% of the rate of CO2 formation
-
-
?
additional information
?
-
-
enzyme functions not as an aldehyde dehydrogenase in vivo, 10-formyltetrahydrofolate hydrolase activity is of no physiological significance, disulfiram may inhibit enzyme activity and probably perturb hepatic folate metabolism in vivo
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-
?
additional information
?
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-
the C-terminal domain (Ct-FDH) of the enzyme is a structural and functional homologue of aldehyde dehydrogenases (ALDHs, EC 1.2.1.4). This domain is capable of catalyzing the NADP+-dependent oxidation of short chain aldehydes to their corresponding acids, and similar to most ALDHs it has two conserved catalytic residues, Cys707 and Glu673. These residues define the conformation of the bound coenzyme and the affinity of its interaction with the protein, proposed mechanism by which Cys707 helps to differentiate between the oxidized and reduced coenzyme during ALDH catalysis, overview
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?
additional information
?
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-
?
additional information
?
-
-
not as substrate: (+)-10-formyltetrahydrofolate
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-
?
additional information
?
-
-
bifunctional enzyme: 10-formyltetrahydrofolate dehydrogenase separated from hydrolase activity, activities are functions of different active sites and take place simultaneously in presence of NADP+
-
-
?
additional information
?
-
-
not as substrate: 5-formyltetrahydrofolate
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-
?
additional information
?
-
-
not as substrate: 5-formyltetrahydrofolate
-
-
?
additional information
?
-
-
enzyme catalyzes hydrolytic cleavage of 10-formyltetrahydrofolate to formate and tetrahydrofolate in absence of NADP+ (15-30% of the rate of oxidative reaction)
-
-
?
additional information
?
-
-
bifunctional protein: 10-formyltetrahydrofolate dehydrogenase/hydrolase, hydrolysis at 20-30% of the oxidative rate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O
tetrahydropteroylhexaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
additional information
?
-
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
enzyme is an important factor in regulation of formate oxidation and is related with methanol poisoning
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
folate-dependent metabolism of formate to carbon dioxide
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate and of the purine biosynthesis through control of the level of 10-formyltetrahydrofolate, down-regulation of FDH in tumors is one of the cellular mechanisms that enhance proliferation, FDH possesses tumor specific suppressor effects
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
folate-dependent pathway is the exclusive route of formate metabolism in primates, plays major role in disposition of formate generated from one-carbon moieties of environmental chemicals, drugs, and foods, importance in the toxicity of methanol
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
a major liver enzyme, contributing to more than one metabolic pathway, regeneration of the tetrahydrofolate pool, not essential for viability
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
ir
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate in the cell in response to yet unknown aldehyde and thiol metabolites
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
natural substrate
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
recycling of excess 10-formyltetrahydrofolate that is not needed for purine biosynthesis and restoration of the tetrahydrofolate pool, important for formate metabolism by clearing it as CO2 and thus protecting cells from formate intoxication
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
regulatory mechanism to control the in vivo folate pool size
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
disposal of excess one-carbon units, oxidation of one-carbon moieties is regulated by the ratio of formyltetrahydrofolate to tetrahydrofolate in liver, regulation of the proportion of folate present in the tetrahydrofolate form, presumably to make it available for other reactions of one-carbon metabolism
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
folate-dependent metabolism of formate to carbon dioxide
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
a major folate-binding protein of liver cytosol, 10-formyltetrahydrofolate polyglutamates are tightly bound in vivo
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
-
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
disposal of excess one-carbon units, oxidation of one-carbon moieties is regulated by the ratio of formyltetrahydrofolate to tetrahydrofolate in liver, regulation of the proportion of folate present in the tetrahydrofolate form, presumably to make it available for other reactions of one-carbon metabolism
-
?
10-formyltetrahydrofolate + NADP+ + H2O
tetrahydrofolate + CO2 + NADPH + H+
-
major disposal route for excess one-carbon units produced in folate-mediated metabolism
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
important site of binding of folylpolyglutamates in liver, regulation of the interconversion of 10-formyltetrahydropteroylpolyglutamate to tetrahydropteroylpolyglutamate and therefore of the high-energy formyl charge of the cell
-
ir
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
natural substrate
-
?
additional information
?
-
-
FDH-expressing cells show accumulation of cells in G0-G1 phase and a sharp decrease of cells in S phase. Accumulation of the tumor suppressor protein p53 and its downstream target p21. FDH antiproliferative effects on A549 cells include both G1 cell cycle arrest and caspase-dependent apoptosis
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-
?
additional information
?
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-
activation of p53 tumor suppressor protein-dependent pathways is a general downstream mechanism in response to induction of enzyme expression in p53 functional cancer cells
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-
?
additional information
?
-
-
enzyme functions not as an aldehyde dehydrogenase in vivo, 10-formyltetrahydrofolate hydrolase activity is of no physiological significance, disulfiram may inhibit enzyme activity and probably perturb hepatic folate metabolism in vivo
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-
?
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Acute Kidney Injury
Ursodeoxycholic acid protects against cisplatin-induced acute kidney injury and mitochondrial dysfunction through acting on ALDH1L2.
Adenocarcinoma of Lung
Epigenetic Silencing of ALDH1L1, a Metabolic Regulator of Cellular Proliferation, in Cancers.
Adenocarcinoma of Lung
The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer.
Astrocytoma
Gene expression profiling of NF-1-associated and sporadic pilocytic astrocytoma identifies aldehyde dehydrogenase 1 family member L1 (ALDH1L1) as an underexpressed candidate biomarker in aggressive subtypes.
Breast Neoplasms
Deep Sequencing Revealed a CpG Methylation Pattern Associated With ALDH1L1 Suppression in Breast Cancer.
Breast Neoplasms
Regional methylome profiling reveals dynamic epigenetic heterogeneity and convergent hypomethylation of stem cell quiescence-associated genes in breast cancer following neoadjuvant chemotherapy.
Carcinogenesis
ALDH1L1 and ALDH1L2 Folate Regulatory Enzymes in Cancer.
Carcinogenesis
Decreased expression of ALDH1L1 is associated with a poor prognosis in hepatocellular carcinoma.
Carcinogenesis
Knockout of Putative Tumor Suppressor Aldh1l1 in Mice Reprograms Metabolism to Accelerate Growth of Tumors in a Diethylnitrosamine (DEN) Model of Liver Carcinogenesis.
Carcinogenesis
Reply to Krupenko et al. Comment on "Lee et al. The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer Cancers 2020, 12, 1382".
Carcinoma, Hepatocellular
ALDH1L1 variant rs2276724 and mRNA expression predict post-operative clinical outcomes and are associated with TP53 expression in HBV-related hepatocellular carcinoma.
Carcinoma, Hepatocellular
Decreased expression of ALDH1L1 is associated with a poor prognosis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Knockout of Putative Tumor Suppressor Aldh1l1 in Mice Reprograms Metabolism to Accelerate Growth of Tumors in a Diethylnitrosamine (DEN) Model of Liver Carcinogenesis.
Carcinoma, Non-Small-Cell Lung
Reply to Krupenko et al. Comment on "Lee et al. The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer Cancers 2020, 12, 1382".
Carcinoma, Non-Small-Cell Lung
The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer.
Colonic Neoplasms
Investigation of Schwann cells at neoplastic cell sites before the onset of cancer invasion.
Colonic Neoplasms
[Functional Hypermethylation of ALDH1L1, PLCL2, and PPP2R3A in Colon Cancer].
Dementia
The Therapeutic Targets of Fingolimod (FTY720) Are Involved in Pathological Processes in the Frontal Cortex of Alzheimer's Disease Patients: A Network Pharmacology Study.
dna (cytosine-5-)-methyltransferase deficiency
A necessary role of DNMT3A in endurance exercise by suppressing ALDH1L1-mediated oxidative stress.
Epilepsy
Molecular analysis of acute and chronic reactive astrocytes in the pilocarpine model of temporal lobe epilepsy.
Hallucinations
Identification of blood biomarkers for psychosis using convergent functional genomics.
Hepatitis
ALDH1L1 variant rs2276724 and mRNA expression predict post-operative clinical outcomes and are associated with TP53 expression in HBV-related hepatocellular carcinoma.
Hydrocephalus
Neonatal hydrocephalus is a result of a block in folate handling and metabolism involving 10-formyltetrahydrofolate dehydrogenase.
Hyperthyroidism
Quantification of the carbon flow through the folate-dependent one-carbon pool using radiolabeled histidine: effect of altered thyroid and folate status.
Ischemic Stroke
Genome-Wide Meta-Analysis of Homocysteine and Methionine Metabolism Identifies Five One Carbon Metabolism Loci and a Novel Association of ALDH1L1 with Ischemic Stroke.
Lung Neoplasms
Aldehyde dehydrogenase inhibition combined with phenformin treatment reversed NSCLC through ATP depletion.
Lung Neoplasms
Reply to Krupenko et al. Comment on "Lee et al. The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer Cancers 2020, 12, 1382".
Lung Neoplasms
The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer.
Lymphoma, T-Cell
Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.
Neoplasm Metastasis
ALDH1L1 and ALDH1L2 Folate Regulatory Enzymes in Cancer.
Neoplasm Metastasis
Oxidative stress inhibits distant metastasis by human melanoma cells.
Neoplasms
10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells.
Neoplasms
10-formyltetrahydrofolate dehydrogenase-induced c-Jun-NH2-kinase pathways diverge at the c-Jun-NH2-kinase substrate level in cells with different p53 status.
Neoplasms
Alcohol intake and folate antagonism via CYP2E1 and ALDH1: effects on oral carcinogenesis.
Neoplasms
ALDH1L1 and ALDH1L2 Folate Regulatory Enzymes in Cancer.
Neoplasms
ALDH1L1 inhibits cell motility via dephosphorylation of cofilin by PP1 and PP2A.
Neoplasms
ALDH1L1 variant rs2276724 and mRNA expression predict post-operative clinical outcomes and are associated with TP53 expression in HBV-related hepatocellular carcinoma.
Neoplasms
ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenase.
Neoplasms
Cancer cells activate p53 in response to 10-formyltetrahydrofolate dehydrogenase expression.
Neoplasms
CHIP E3 ligase mediates proteasomal degradation of the proliferation regulatory protein ALDH1L1 during the transition of NIH3T3 fibroblasts from G0/G1 to S-phase.
Neoplasms
Decreased expression of ALDH1L1 is associated with a poor prognosis in hepatocellular carcinoma.
Neoplasms
Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis.
Neoplasms
Epigenetic alterations of chromosome 3 revealed by NotI-microarrays in clear cell renal cell carcinoma.
Neoplasms
Epigenetic Silencing of ALDH1L1, a Metabolic Regulator of Cellular Proliferation, in Cancers.
Neoplasms
Folate Stress Induces Apoptosis via p53-Dependent de novo Ceramide Synthesis and Up-Regulation of Ceramide Synthase 6.
Neoplasms
Gene expression profiling of NF-1-associated and sporadic pilocytic astrocytoma identifies aldehyde dehydrogenase 1 family member L1 (ALDH1L1) as an underexpressed candidate biomarker in aggressive subtypes.
Neoplasms
Investigation of Schwann cells at neoplastic cell sites before the onset of cancer invasion.
Neoplasms
Is ALDH1L1 Elevated in Lung Cancer? Comment on: Lee, S.-H.; et al. "The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer" Cancers 2020, 12, 1382.
Neoplasms
JNK1/2 regulate Bid by direct phosphorylation at Thr59 in response to ALDH1L1.
Neoplasms
Knocking down 10-Formyltetrahydrofolate dehydrogenase increased oxidative stress and impeded zebrafish embryogenesis by obstructing morphogenetic movement.
Neoplasms
Knockout of Putative Tumor Suppressor Aldh1l1 in Mice Reprograms Metabolism to Accelerate Growth of Tumors in a Diethylnitrosamine (DEN) Model of Liver Carcinogenesis.
Neoplasms
Loss of ALDH1L1 folate enzyme confers a selective metabolic advantage for tumor progression.
Neoplasms
Novel tumor suppressor candidates on chromosome 3 revealed by NotI-microarrays in cervical cancer.
Neoplasms
Oxidative stress inhibits distant metastasis by human melanoma cells.
Neoplasms
Reply to Krupenko et al. Comment on "Lee et al. The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer Cancers 2020, 12, 1382".
Neoplasms
The Combination of Loss of ALDH1L1 Function and Phenformin Treatment Decreases Tumor Growth in KRAS-Driven Lung Cancer.
Neoplasms
The one-carbon metabolism pathway highlights therapeutic targets for gastrointestinal cancer (Review).
Neoplasms
The Role of Single-Nucleotide Polymorphisms in the Function of Candidate Tumor Suppressor ALDH1L1.
Neoplasms
Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.
Neural Tube Defects
Association between ALDH1L1 gene polymorphism and neural tube defects in the Chinese Han population.
Neural Tube Defects
The folate metabolic enzyme ALDH1L1 is restricted to the midline of the early CNS, suggesting a role in human neural tube defects.
Neuroblastoma
Involvement of aldehyde dehydrogenase 1A2 in the regulation of cancer stem cell properties in neuroblastoma.
Ovarian Neoplasms
Prognostic values of aldehyde dehydrogenase 1 isoenzymes in ovarian cancer.
Prostatic Neoplasms
JNK1/2 regulate Bid by direct phosphorylation at Thr59 in response to ALDH1L1.
Protein Deficiency
Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice.
Spinal Dysraphism
An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1).
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Kutzbach, C.; Stokstad, E.L.R.
10-Formyl tetrahydrofolate:NADP oxidoreductase
Methods Enzymol.
18B
793-798
1971
Gallus gallus, Rattus norvegicus, Sus scrofa
-
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Case, G.L.; Kaisaki, P.J.; Steele, R.D.
Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase activities
J. Biol. Chem.
263
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1988
Rattus norvegicus
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Rios-Orlandi, E.M.; Zarkadas, C.G.; MacKenzie, R.E.
Formyltetrahydrofolate dehydrogenase-hydrolase from pig liver: simultaneous assay of the activities
Biochim. Biophys. Acta
871
24-35
1986
Sus scrofa
brenda
Kutzbach, C.; Stokstad, E.L.R.
Partial purification of a 10-formyl-tetrahydrofolate: NADP oxidoreductase from mammalian liver
Biochem. Biophys. Res. Commun.
30
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1968
Sus scrofa
brenda
Min, H.; Shane, B.; Stokstad, E.L.R.
Identification of 10-formyltetrahydrofolate dehydrogenase-hydrolase as a major folate binding protein in liver cytosol
Biochim. Biophys. Acta
967
348-353
1988
Rattus norvegicus, Sus scrofa
brenda
Johlin, F.C.; Swain, E.; Smith, C.; Tephly, T.R.
Studies on the mechanism of methanol poisoning: purification and comparison of rat and human liver 10-formyltetrahydrofolate dehydrogenase
Mol. Pharmacol.
35
745-750
1989
Homo sapiens, Rattus norvegicus
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Scrutton, M.C.; Beis, I.
Inhibitory effects of histidine and their reversal. The roles of pyruvate carboxylase and N10-formyltetrahydrofolate dehydrogenase
Biochem. J.
177
833-846
1979
Rattus norvegicus
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Cook, R.J.; Wagner, C.
Enzymatic activities of rat liver cytosol 10-formyltetrahydrofolate dehydrogenase
Arch. Biochem. Biophys.
321
336-344
1995
Oryctolagus cuniculus, Rattus norvegicus
brenda
Wagner, C.; Briggs, W.T.; Horne, D.H.; Cook, R.J.
10-Formyltetrahydrofolate dehydrogenase: Identification of the natural folate ligand, covalent labeling, and partial tryptic digestion
Arch. Biochem. Biophys.
316
141-147
1995
Rattus norvegicus, Sus scrofa
brenda
Schirch, D.; Villar, E.; Maras, B.; Barra, D.; Schirch, V.
Domain structure and function of 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
269
24728-24735
1994
Oryctolagus cuniculus
brenda
Krupenko, S.A.; Wagner, C.
Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
274
35777-35784
1999
Rattus norvegicus
brenda
Krupenko, S.A.; Vlasov, A.P.; Wagner, C.
On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis
J. Biol. Chem.
276
24030-24037
2001
Rattus norvegicus
brenda
Krupenko, S.A.; Wagner, C.
Overexpression of functional hydrolase domain of rat liver 10-formyltetrahydrofolate dehydrogenase in Escherichia coli
Protein Expr. Purif.
14
146-152
1998
Rattus norvegicus
brenda
Hong, M.; Lee, Y.; Kim, J.W.; Lim, J.S.; Chang, S.Y.; Lee, K.S.; Paik, S.G.; Choe, I.S.
Isolation and characterization of cDNA clone for human liver 10-formyltetrahydrofolate dehydrogenase
Biochem. Mol. Biol. Int.
47
407-415
1999
Homo sapiens
brenda
Kim, D.W.; Huang, T.; Schirch, D.; Schirch, V.
Properties of tetrahydropteroylpentaglutamate bound to 10-formyltetrahydrofolate dehydrogenase
Biochemistry
35
15772-15783
1996
Oryctolagus cuniculus
brenda
Krupenko, S.A.; Oleinik, N.V.
10-Formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells
Cell Growth Differ.
13
227-236
2002
Homo sapiens, Rattus norvegicus
brenda
Krupenko, S.A.; Wagner, C.; Cook, R.J.
Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate
Biochem. J.
306
651-655
1995
Rattus norvegicus
-
brenda
Kim, S.; Park, G.H.; Joo, W.A.; Paik, W.K.; Cook, R.J.; Williams, K.R.
Identification of protein-arginine N-methyltransferase as 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
273
27374-27382
1998
Rattus norvegicus
brenda
Krupenko, S.A.; Wagner, C.; Cook, R.J.
Cysteine 707 is involved in the dehydrogenase active site of rat 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
270
519-522
1995
Rattus norvegicus
brenda
Champion, K.M.; Cook, R.J.; Tollaksen, S.L.; Giometti, C.S.
Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice
Proc. Natl. Acad. Sci. USA
91
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1994
Mus musculus
brenda
Martinasevic, M.K.; Green, M.D.; Baron, J.; Tephly, T.R.
Folate and 10-formyltetrahydrofolate dehydrogenase in human and rat retina: Relation to methanol toxicity
Toxicol. Appl. Pharmacol.
141
373-381
1996
Homo sapiens, Rattus norvegicus
brenda
Chumanevich, A.A.; Krupenko, S.A.; Davies, C.
The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain
J. Biol. Chem.
279
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2004
Rattus norvegicus (P28037)
brenda
Reuland, S.N.; Vlasov, A.P.; Krupenko, S.A.
Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains
J. Biol. Chem.
278
22894-22900
2003
Rattus norvegicus (P28037)
brenda
Oleinik, N.V.; Krupenko, S.A.
Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis
Mol. Cancer Res.
1
577-588
2003
Homo sapiens
brenda
Min, H.; Im, E.S.; Seo, J.S.; Mun, J.A.; Burri, B.J.
Effects of chronic ethanol ingestion and folate deficiency on the activity of 10-formyltetrahydrofolate dehydrogenase in rat liver
Alcohol. Clin. Exp. Res.
29
2188-2193
2005
Rattus norvegicus
brenda
Oleinik, N.V.; Krupenko, N.I.; Priest, D.G.; Krupenko, S.A.
Cancer cells activate p53 in response to 10-formyltetrahydrofolate dehydrogenase expression
Biochem. J.
391
503-511
2005
Homo sapiens
brenda
Kim, H.S.; Kim, J.M.; Roh, K.B.; Lee, H.H.; Kim, S.J.; Shin, Y.H.; Lee, B.L.
Rat liver 10-formyltetrahydrofolate dehydrogenase, carbamoyl phosphate synthetase 1 and betaine homocysteine S-methytransferase were co-purified on Kunitz-type soybean trypsin inhibitor-coupled sepharose CL-4B
J. Biochem. Mol. Biol.
40
604-609
2007
Rattus norvegicus
brenda
Tsybovsky, Y.; Donato, H.; Krupenko, N.I.; Davies, C.; Krupenko, S.A.
Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases
Biochemistry
46
2917-2929
2007
Rattus norvegicus
brenda
Donato, H.; Krupenko, N.I.; Tsybovsky, Y.; Krupenko, S.A.
10-formyltetrahydrofolate dehydrogenase requires a 4-phosphopantetheine prosthetic group for catalysis
J. Biol. Chem.
282
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2007
Rattus norvegicus
brenda
McNeil, C.J.; Hay, S.M.; Rucklidge, G.J.; Reid, M.; Duncan, G.; Maloney, C.A.; Rees, W.D.
Disruption of lipid metabolism in the liver of the pregnant rat fed folate-deficient and methyl donor-deficient diets
Br. J. Nutr.
99
262-271
2008
Rattus norvegicus (P28037)
brenda
Strickland, K.C.; Hoeferlin, L.A.; Oleinik, N.V.; Krupenko, N.I.; Krupenko, S.A.
Acyl carrier protein-specific 4-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
285
1627-1633
2010
Homo sapiens
brenda
Krupenko, N.I.; Dubard, M.E.; Strickland, K.C.; Moxley, K.M.; Oleinik, N.V.; Krupenko, S.A.
ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
285
23056-23063
2010
Homo sapiens (O75891), Homo sapiens (Q3SY69), Homo sapiens
brenda
Ghose, S.; Oleinik, N.V.; Krupenko, N.I.; Krupenko, S.A.
10-formyltetrahydrofolate dehydrogenase-induced c-Jun-NH2-kinase pathways diverge at the c-Jun-NH2-kinase substrate level in cells with different p53 status
Mol. Cancer Res.
7
99-107
2009
Homo sapiens
brenda
Chang, W.N.; Lin, H.C.; Fu, T.F.
Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties
Protein Expr. Purif.
72
217-222
2010
Danio rerio (E3NZ06), Danio rerio
brenda
Strickland, K.C.; Krupenko, N.I.; Dubard, M.E.; Hu, C.J.; Tsybovsky, Y.; Krupenko, S.A.
Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate dehydrogenase
Chem. Biol. Interact.
191
129-136
2011
Homo sapiens
brenda
Tsybovsky, Y.; Malakhau, Y.; Strickland, K.C.; Krupenko, S.A.
The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1
Chem. Biol. Interact.
202
62-69
2013
Rattus norvegicus
brenda