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Information on EC 1.5.1.6 - formyltetrahydrofolate dehydrogenase and Organism(s) Rattus norvegicus and UniProt Accession P28037
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1.5.1.6 formyltetrahydrofolate dehydrogenaseSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aldh1l1, 10-formyltetrahydrofolate dehydrogenase, aldh1l2, 10-fthfdh, formyltetrahydrofolate dehydrogenase, mtfdh, 10-fdh, 10-formyl-h4folate dehydrogenase, 10-fthf dehydrogenase, n10-formyltetrahydrofolate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10-FDH
-
-
-
-
10-formyl tetrahydrofolate:NADP oxidoreductase
-
-
-
-
10-formyl-H2PtGlu:NADP oxidoreductase
-
-
-
-
10-formyl-H4folate dehydrogenase
-
-
-
-
10-formyltetrahydrofolate dehydrogenase
10-FTHFDH
-
-
-
-
dehydrogenase, formyltetrahydrofolate
-
-
-
-
FBP-CI
-
-
-
-
FBP-CI proteins
-
-
-
-
FDH
folate-binding proteins, cytosol I
-
-
-
-
N10-formyltetrahydrofolate dehydrogenase
-
-
-
-
proteins, folate-binding, cytosol I
-
-
-
-
additional information
10-formyltetrahydrofolate dehydrogenase
-
-
-
-
FDH
-
-
-
-
additional information
-
identical with folate binding protein cytosol-I, FBP-CI
additional information
-
identical with folate binding protein cytosol-I, FBP-CI
additional information
-
identical with protein-arginine methyltransferase from liver cytosol, EC 2.1.1.23
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+
reaction mechanism
-
10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+
sequential mechanism of substrate addition
-
10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+
FDH catalyzes the hydrolytic cleavage of the formyl group in the N-terminal catalytic domain, followed by NADP+-dependent oxidation of the formyl group toCO2 in the C-terminal aldehyde dehydrogenase domain
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
oxidation
reduction
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
10-formyltetrahydrofolate:NADP+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
37256-25-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
-
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
-
-
-
-
?
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+
-
-
-
?
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-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
natural 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
?
-
-
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
-
-
?
additional information
?
-
-
bifunctional enzyme: NADP+-dependent dehydrogenase activity and NADP+-independent hydrolase activity of 10-formyltetrahydrofolate with two active sites
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
bifunctional protein: 10-formyltetrahydrofolate dehydrogenase/hydrolase, hydrolysis at 20-30% of the oxidative rate
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
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
-
-
?
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-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
-
-
?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
tetrahydropteroylpentaglutamate + CO2 + NADPH
-
natural substrate
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-formyltetrahydrofolate
-
covalent linkage of 5-formyltetrahydrofolate to enzyme, 2 mol bound per mol of enzyme monomer, it is a minor form of the folate coenzymes and arises from 10-formyltetrahydrofolate
10-formyltetrahydrofolate
-
10-formyltetrahydrofolate
392335, 392336, 392339, 392340, 392341, 392342, 392343, 392345, 392346, 392347, 392350, 392351, 392352, 392353, 392355
10-formyltetrahydrofolate
-
10-formyltetrahydrofolate is one of the most labile of the reduced coenzymes
folate
-
2 mol of folate bound per mol of enzyme monomer, consistent with the presence of two active sites
NADP+
-
NADP+-dependent
NADP+
-
binding of substrate, 10-formyltetrahydrofolate or propanal, influences enzyme affinity for NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
propanal
-
FDH activity decreases with increasing concentrations, competes with 10-formyltetrahydrofolate for NADP+-dependent oxidation
tetrahydrofolate
-
competitive to 10-formyltetrahydrofolate and non-competitive to NADP+
Trypsin
-
tryptic digestion inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase activity
-
Trypsin
-
20 min, 70% inhibition, rapid but incomplete loss of dehydrogenase activity
-
additional information
-
not inhibited by the folate analog N-[4-[[3-(2,4-diamino-1,6-dihydro-6-oxo-5-pyrimidinyl)propyl]amino]-benzoyl]-L-glutamate
-
additional information
-
recombinant FDH is not inhibited by sodium azide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
activates at concentrations and in ratio with NADP+ consistent with those in rat liver in vivo, activation is associated with higher Ki-value for tetrahydrofolate
2-mercaptoethanol
-
5 to 15 mM: 1.7fold increase in activity, higher concentrations have no further effect, it may reduce oxidized Cys-707 or another important sulfhydryl group
2-mercaptoethanol
-
dehydrogenase and hydrolase activities are dependent on the presence of high concentrations of 2-mercaptoethanol to prevent the oxidative degradation of the substrate 10-formyltetrahydrofolate
2-mercaptoethanol
-
optimal dehydrogenase activity requires 15 mM or higher concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
much lower levels than in liver, preferentially localized in Müller cells, FDH levels in human retina are higher than in rat retina, folate levels in human retina are 14% of those in rat retina
-
-
392335, 392336, 392339, 392341, 392342, 392343, 392345, 392346, 392347, 392351, 392352, 392353, 392355, 674389
-
activity in human liver is 26% of that in rat liver, reduced amount of enzyme in human liver
-
feeding of ethanol decreases hepatic enzyme activity, decrease occurs irrespective of folate status
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
not detected in nucleus, lysosomes or peroxisomes
-
-
comparable amounts of cytosolic and mitochondrial FDH in retinal tissues
-
comparable amounts of cytosolic and mitochondrial FDH in retinal tissues
-
small amount, 0.4% of total liver dehydrogenase activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AL1L1_RAT
902
0
98874
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
393200
-
C707A mutant FDH, molecular size detector employing laser-light scattering methodology
398800
-
wild-type FDH, molecular size detector employing laser-light scattering methodology
99000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
FDH requires posttranslational modification to become a functional enzyme (4'-phosphopantetheine prosthetic group)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the hydrolase domain of FDH, solved to 2.3 A resolution
C-terminal domain of FDH and its complexes with oxidized and reduced forms of NADP+ are crystallized using the hanging drop vapour diffusion method with 1.4-1.5 M ammonium sulfate and 0.1 M Tris-HCl, pH 7.0-7.5
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C707A
D142A
-
mutant with a complete loss of 10-formyltetrahydrofolate dehydrogenase and hydrolase activity, aldehyde dehydrogenase activity is similar to wild-type FDH
H106K
-
mutant with a complete loss of 10-formyltetrahydrofolate dehydrogenase and hydrolase activity, aldehyde dehydrogenase activity is similar to wild-type FDH
C707A
-
mutant with a complete loss of NADP+-dependent 10-formyltetrahydrofolate dehydrogenase activity, but no influence on hydrolase activity
C707A
-
mutant with a complete loss of dehydrogenase activity of 10-formyltetrahydrofolate and propanal, but hydrolase activity and binding of NADP+ is unchanged
C707A
-
site-directed mutagenesis of the C-terminal residue, replacement of Cys707 with an alanine results in the enzyme lacking the ability to differentiate between the oxidized and reduced coenzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
prone to oxidative inactivation, but may be partially reactivated by incubation with 100 mM 2-mercaptoethanol or 100 mM dithiothreitol
-
392342
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 0.05 M phosphate buffer, pH 7.2, 50%-saturated (NH4)2SO4, 20% glycerol, 1 mM EDTA, 0.1 mM dithioerythritol, 0.01 mM phenylmethanesulfonyl fluoride, several months, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5-fTHFSepharose column chromatography, Sephacryl S-300 gel filtration, and MonoQ column chromatography
-
co-purification with carbamoyl-phosphate synthetase 1 and betaine homocysteine S-methyltransferase using Kunitz-type soybean trypsin inhibitor-coupled Sepharose CL-4B column chromatography, Sephacryl S-200 gel filtration, and Superdex 200 gel filtration
-
Kunitz-type soybean trypsin inhibitor-coupled Sepharose CL-4B column chromatography
-
separated from 10-formyltetrahydrofolate hydrolase, dehydrogenase and hydrolase are closely related and separately compartmentalized enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
clone expressed in insect cells has both dehydrogenase and hydrolase activity and exhibits almost identical kinetic parameters to the native rat liver enzyme
-
expression of D124A mutant of FDH and N-terminal domain mutants in Sf9 insect cells, using a baculovirus expression system
-
expression of FDH and its N-terminal and C-terminal domains in insect cells, using a baculovirus expression system, expression of FDH and of its 310 amino acid residue N-terminal domain in Escherichia coli BL21 using the pRSET vector, full-length enzyme expressed in Escherichia coli is nonsoluble, because of the large size of its monomer and uncorrect folding in prokaryotic cells
-
expression of FDH cDNA, subcloned in the pVL 1393 baculovirus vector, in Sf9 insect cells, using the MaxBac expression system
-
expression of FDH in insect cells using the pVL 1393 baculovirus expression vector
-
expression of H106K mutant of FDH in insect cells SF9, using a baculovirus expression system, and of N-terminal domain mutants in Escherichia coli BL 21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
feeding of ethanol decreases hepatic enzyme activity, decrease occurs irrespective of folate status
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kutzbach, C.; Stokstad, E.L.R.
10-Formyl tetrahydrofolate:NADP oxidoreductase
Methods Enzymol.
18B
793-798
1971
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Rattus norvegicus
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Rattus norvegicus, Sus scrofa
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Oryctolagus cuniculus, Rattus norvegicus
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Rattus norvegicus, Sus scrofa
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Rattus norvegicus
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Rattus norvegicus
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Rattus norvegicus
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10-Formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells
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Homo sapiens, Rattus norvegicus
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Rattus norvegicus
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Rattus norvegicus
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Homo sapiens, Rattus norvegicus
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Rattus norvegicus (P28037)
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Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains
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Rattus norvegicus (P28037)
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Rattus norvegicus
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
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Rattus norvegicus
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
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2007
Rattus norvegicus
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10-formyltetrahydrofolate dehydrogenase requires a 4-phosphopantetheine prosthetic group for catalysis
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Rattus norvegicus
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Rattus norvegicus (P28037)
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