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Information on EC 1.5.1.3 - dihydrofolate reductase and Organism(s) Mus musculus and UniProt Accession P00375
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1.5.1.3 dihydrofolate reductaseIUBMB Comments
The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
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Word Map
- 1.5.1.3
- methotrexate
- antifolate
- plasmodium
- falciparum
- hamster
- malaria
- pyrimethamine
- ovary
-
antimalarial
- leukemia
- dihydropteroate
- thymidine
- pyrimidine
- carinii
- polyglutamates
- pneumocystis
-
hydride
- chloroquine
-
casey
-
drug-resistant
- tmp
-
ccrf-cem
- vivax
- glycinamide
- toxoplasma
-
uncomplicated
-
folate-dependent
- mthfr
- folylpolyglutamate
- pemetrexed
-
sublines
- leucovorin
- tetrahydrobiopterin
-
polyglutamylation
- gondii
-
nontranscribed
- sulfamethoxazole
- trimethoprim-sulfamethoxazole
- quinazoline
- 5-methyltetrahydrofolate
- sepiapterin
- integrons
- dihydropteridine
- analysis
- medicine
- artesunate
- synthesis
-
triazine
-
folinic
- 5,10-methylenetetrahydrofolate
- bh4
- biotechnology
- biopterins
- drug development
- pterins
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
dhfr, dihydrofolate reductase, thy-1, dhfr-ts, hdhfr, dihydrofolate reductase-thymidylate synthase, ecdhfr, pcdhfr, r67 dhfr, ts-dhfr, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7,8-dihydrofolate reductase
-
-
-
-
dehydrogenase, tetrahydrofolate
-
-
-
-
DHFR
DHFR type IIIC
-
-
-
-
dihydrofolate reductase-thymidylate synthase
-
-
-
-
dihydrofolate reductase:thymidylate synthase
-
-
-
-
dihydrofolic acid reductase
-
-
-
-
dihydrofolic reductase
-
-
-
-
folic acid reductase
-
-
-
-
folic reductase
-
-
-
-
NADPH-dihydrofolate reductase
-
-
-
-
pteridine reductase:dihydrofolate reductase
-
-
-
-
reductase, dihydrofolate
-
-
-
-
tetrahydrofolate dehydrogenase
-
-
-
-
thymidylate synthetase-dihydrofolate reductase
-
-
-
-
Trimethoprim resistance protein
-
-
-
-
DHFR
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
inhibitor binding mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase
The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
CAS REGISTRY NUMBER
COMMENTARY
9002-03-3
-
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
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
r
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
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
organic mercurials
-
animal enzyme: activated, bacterial enzyme: unaffected or inhibited
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine
crystallization data
4-([5-[(2,4-diaminopteridin-6-yl)methyl]-5H-dibenzo[b,f]azepin-2-yl]oxy)butane-1,1-diol
O-(3-carboxypropyl) inhibitor, crystallization data
(E)-5-[2-(2-methoxyphenyl)prop-1-en-1-yl]furo[2,3-d]pyrimidine-2,4-diamine
-
DHFR binding structure, modelling, overview
(Z)-5-[2-(2-methoxyphenyl)prop-1-en-1-yl]furo[2,3-d]pyrimidine-2,4-diamine
-
DHFR binding structure, modelling, overview
5-[(R/S)-2-(2'-methoxyphenyl)-3-methylbutyl]furo[2,3-d]-pyrimidine-2,4-diamine
-
-
5-[(R/S)-2-(2'-methoxyphenyl)-3-methylpentyl]furo[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(R/S)-2-(2'-methoxyphenyl)-4-methylpentyl]furo[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(R/S)-2-cyclopropyl-2-(2'-methoxyphenyl)ethyl]furo-[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(Z/E)-2-(2'-methoxyphenyl)-3-methylbut-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(Z/E)-2-(2'-methoxyphenyl)-3-methylpent-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(Z/E)-2-(2'-methoxyphenyl)-4-methylpent-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(Z/E)-2-(2'-methoxyphenyl)hex-1-en-1-yl]furo[2,3-d]-pyrimidine-2,4-diamine
-
-
5-[(Z/E)-2-(2'-methoxyphenyl)pent-1-en-1-yl]furo[2,3-d]-pyrimidine-2,4-diamine
-
-
5-[(Z/E)-2-cyclopropyl-2-(2'-methoxyphenyl)vinyl]furo-[2,3-d]pyrimidine-2,4-diamine
-
-
methotrexate
-
biphasic inhibition at pH 7.0, competitive against 7,8-dihydrofolate
additional information
-
synthesis and evaluation of 2,4-diaminofuro[2,3-d]pyrimidine inhibitors, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km of enzymes with decreased binding of folate and antagonists and of drug-sensitive enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000062
(E)-5-[2-(2-methoxyphenyl)prop-1-en-1-yl]furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00016
(Z)-5-[2-(2-methoxyphenyl)prop-1-en-1-yl]furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00006
5-[(R/S)-2-(2'-methoxyphenyl)-3-methylbutyl]furo[2,3-d]-pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00078
5-[(R/S)-2-(2'-methoxyphenyl)-3-methylpentyl]furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00062
5-[(R/S)-2-(2'-methoxyphenyl)-4-methylpentyl]furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.0033
5-[(R/S)-2-(2'-methoxyphenyl)hexyl]furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.0028
5-[(R/S)-2-(2'-methoxyphenyl)pentyl]furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00006
5-[(R/S)-2-cyclopropyl-2-(2'-methoxyphenyl)ethyl]furo-[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00007
5-[(Z/E)-2-(2'-methoxyphenyl)-3-methylbut-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00007
5-[(Z/E)-2-(2'-methoxyphenyl)-3-methylpent-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00091
5-[(Z/E)-2-(2'-methoxyphenyl)-4-methylpent-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00055
5-[(Z/E)-2-(2'-methoxyphenyl)hex-1-en-1-yl]furo[2,3-d]-pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00014
5-[(Z/E)-2-(2'-methoxyphenyl)pent-1-en-1-yl]furo[2,3-d]-pyrimidine-2,4-diamine
-
pH 7.4, 37°C
0.00008
5-[(Z/E)-2-cyclopropyl-2-(2'-methoxyphenyl)vinyl]furo-[2,3-d]pyrimidine-2,4-diamine
-
pH 7.4, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0039
(E)-5-[2-(2-methoxyphenyl)prop-1-en-1-yl]furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0145
(Z)-5-[2-(2-methoxyphenyl)prop-1-en-1-yl]furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0032
5-[(R/S)-2-(2'-methoxyphenyl)-3-methylbutyl]furo[2,3-d]-pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0445
5-[(R/S)-2-(2'-methoxyphenyl)-3-methylpentyl]furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0354
5-[(R/S)-2-(2'-methoxyphenyl)-4-methylpentyl]furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.187
5-[(R/S)-2-(2'-methoxyphenyl)hexyl]furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.162
5-[(R/S)-2-(2'-methoxyphenyl)pentyl]furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0037
5-[(R/S)-2-cyclopropyl-2-(2'-methoxyphenyl)ethyl]furo-[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0041
5-[(Z/E)-2-(2'-methoxyphenyl)-3-methylbut-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0042
5-[(Z/E)-2-(2'-methoxyphenyl)-3-methylpent-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0519
5-[(Z/E)-2-(2'-methoxyphenyl)-4-methylpent-1-en-1-yl]-furo[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0312
5-[(Z/E)-2-(2'-methoxyphenyl)hex-1-en-1-yl]furo[2,3-d]-pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0079
5-[(Z/E)-2-(2'-methoxyphenyl)pent-1-en-1-yl]furo[2,3-d]-pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
0.0046
5-[(Z/E)-2-cyclopropyl-2-(2'-methoxyphenyl)vinyl]furo-[2,3-d]pyrimidine-2,4-diamine
Mus musculus
-
pH 7.4, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.005
liver cell mitochondria, pH 7.5, temperature not specified in the publication
0.044
mitochondria of cancer cell line 4T1, pH 7.5, temperature not specified in the publication
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
methotrexate resistant cells L1210 (R), sarcoma 180 (AT/300), 2 optima: pH 4 and pH 7.5
7.5
-
methotrexate resistant cells, L1210(R), sarcoma 180 (AT/30000), 2 optima: pH 4.0 and pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the source of mitochondrial DHFR activity is parental DHFR in mouse
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
identification of a second functional dihydrofolate reductase enzyme in humans, DHFRL1. RNA-mediated DHFR duplication events occur across the mammal tree. Dihydrofolate reductase activity is also a feature of the mitochondria in both rat and mouse but this is not due to a second enzyme. Humans have evolved the need for two separate enzymes, while laboratory rats and mice have just one. RNA-mediated DHFR duplicates in brown rat and mouse are likely to be processed pseudogenes
physiological function
dihydrofolate reductase (DHFR) is an enzyme from the folate one-carbon metabolism pathway that plays a role in drug resistance and in reducing the synthetic supplement folic acid and 7,8-dihydrofolate to the active form, tetrahydrofolate
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). DYR_MOUSE
187
0
21606
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
1 * 21460, methotrexate resistant L1210 (R) cells, amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
holo and ternary complexes with NADPH and the inhibitor 2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine, to 1.9 and 1.4 A resolution, respectively. Modeling data of inhibitor 4-([5-[(2,4-diaminopteridin-6-yl)methyl]-5H-dibenzo[b,f]azepin-2-yl]oxy)butane-1,1-diol in the active site indicate that binding would require ligand-induced conformational changes to the enzyme for the inhibitor to fit or that the inhibitor side-chain would have to adopt an alternative binding mode to that observed for similar inhibitors. The complexes have a decreased active-site volume compared with complexes of the enzyme from Pneumocystis carinii
wild-type and mutant L22R in ternary complex with methotrexate and NADPH, comparison with human anologues. Active site of mouse enzyme is larger than that of human enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
incorporation of an alkyne-bearing non-natural amino acid, p-ethynylphenylalanine, into murine dihydrofolate reductase (mDHFR) at Val43, in high cell density cultivation of Escherichia coli, and performance of Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) conjugation with fluorescent azide dyes to evaluate enzyme compatibility with various CuAAC conditions comprising combination of commercially available Cu(I)-chelating ligands and reductants. The condensed culture improves the protein yield 19fold based on the same amount of non-natural amino acid. Enzyme incubation under optimized reaction condition does not lead to any activity loss but allows a fast and high-yield bioconjugation. Using the established conditions, a biotin-azide spacer is efficiently conjugated to enzyme mDHFR with retained activity leading to the site-specific immobilization of the biotin-conjugated mDHFR on a streptavidin-coated plate. Method evaluation, overview
additional information
-
incorporation of an alkyne-bearing non-natural amino acid, p-ethynylphenylalanine, into murine dihydrofolate reductase (mDHFR) at Val43, in high cell density cultivation of Escherichia coli, and performance of Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) conjugation with fluorescent azide dyes to evaluate enzyme compatibility with various CuAAC conditions comprising combination of commercially available Cu(I)-chelating ligands and reductants. The condensed culture improves the protein yield 19fold based on the same amount of non-natural amino acid. Enzyme incubation under optimized reaction condition does not lead to any activity loss but allows a fast and high-yield bioconjugation. Using the established conditions, a biotin-azide spacer is efficiently conjugated to enzyme mDHFR with retained activity leading to the site-specific immobilization of the biotin-conjugated mDHFR on a streptavidin-coated plate. Method evaluation, overview
additional information
-
selection of cell line with altered enzyme due to decreased methotrexate-sensitivity
additional information
-
transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type mDHFR and modified mDHFR-43pEthF enzymes from Escherichia coli strain XL1-Blue by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a dihydrofolate reductase-like sequence, DHFRLS, is encoded on chromosome 9, orf 31567433:31568480, phylogenetic analysis and tree, quantitative RT-PCR enzyme expression analysis
recombinant expression of His-tagged wild-type mDHFR and modified mDHFR-43pEthF enzymes in Escherichia coli strain XL1-Blue
transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of a survival protein-fragment complementation assay based on dihydrofolate reductase. Proteins of interest are fused to complementary fragments of dihydrofolate reductase. If the proteins of interst interact physically, the dihydrofolate complementary fragments are brought together and fold into the native structure, reconstituting its activity
synthesis
synthesis
-
develoment of a method for bacterial expression of mouse translation factor eIF4E tagged with mutant dihydrofolate reductase. Recombinant eIF4E and DHFR-eIF4E both show to significantly enhance in vitro translation in dose dependent manner by 75% at 0.0005 mM. Increased concentrations of eIF4E and DHFR-eIF4E significantly inhibit translation in a dose dependent manner by a maximum at 0.0022 mM of 60% and 90%, respectively
synthesis
-
transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kraut, J.; Matthews, D.A.
Dihydrofolate reductase
Biol. Macromol. and Assem. (Junak, F. , McPherson, eds. )
3
1-71
1987
Klebsiella aerogenes, Bacteria, Gallus gallus, Escherichia coli, Homo sapiens, Lacticaseibacillus casei, Mus musculus, Pigeon, protozoa, vertebrata
-
Freisheim, J.H.; Matthews, D.A.
The comparative biochemistry of dihydrofolate reductase
Folate Antagonists Ther. Agents (Sirotnak, F. M. , ed. )
1
69-131
1984
Bacteria, Tequatrovirus T4, Bos taurus, Gallus gallus, Crithidia fasciculata, Streptococcus pneumoniae, Escherichia coli, Enterococcus faecium, Homo sapiens, Lacticaseibacillus casei, Mammalia, Mus musculus, protozoa, Sus scrofa, vertebrata
-
Baker, B.R.
Tissue-specific irreversible inhibitors of dihydrofolic reductase
Acc. Chem. Res.
2
129-136
1969
Mus musculus, Pigeon, Rattus norvegicus
-
Chello, P.L.; Cashmore, A.R.; Jacobs, S.A.; Bertino, J.R.
Improved purification of tetrahydrofolate dehydrogenase from L1210 leukemia by affinity chromatography
Biochim. Biophys. Acta
268
30-34
1972
Mus musculus
Kaufman, B.T.
Methotrexate-agarose in the purification of dihydrofolate reductase
Methods Enzymol.
34
272-281
1974
Tequatrovirus T4, Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Cricetulus sp., Escherichia coli, Lacticaseibacillus casei, Mus musculus, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
Gauldie, J.; Hillicoat, B.L.
Purification of tetrahydrofolate dehydrogenase by affinity chromatography
Biochim. Biophys. Acta
268
35-40
1972
Mus musculus
Huennekens, F.M.; Vitols, K.S.; Whiteley, J.M.; Neef, V.G.
Dihydrofolate reductase
Methods Cancer Res.
13
199-225
1976
Tequatrovirus T4, Bos taurus, Gallus gallus, Cricetulus sp., Escherichia coli, Enterococcus faecalis, Enterococcus faecium, Lacticaseibacillus casei, Mammalia, Mus musculus, Sus scrofa
-
Fan, C.C.; Vitols, K.S.; Huennekens, F.M.
Inhibition of dihydrofolate reductase by methotrexate: a new look at an old problem
Adv. Enzyme Regul.
18
41-52
1980
Mus musculus
Gupta, S.V.; Greenfield, N.J.; Poe, M.; Makulu, D.R.; Williams, M.N.; Moroson, B.A.; Bertino, J.R.
Dihydrofolate reductase from a resistant subline of the L1210 lymphoma. Purification by affinity chromatography and ultraviolet difference spectrophotometric and circular dichroic studies
Biochemistry
16
3073-3079
1977
Mus musculus
Haber, D.A.; Beverley, S.M.; Kiely, M.L.; Schimke, R.T.
Properties of an altered dihydrofolate reductase encoded by amplified genes in cultured mouse fibroblasts
J. Biol. Chem.
256
9501-9510
1981
Mus musculus
Cody, V.; Luft, J.R.; Pangborn, W.
Understanding the role of Leu22 variants in methotrexate resistance: comparison of wild-type and Leu22Arg variant mouse and human dihydrofolate reductase ternary crystal complexes with methotrexate and NADPH
Acta crystallogr. Sect. D
61
147-155
2005
Homo sapiens, Mus musculus
Cody, V.; Pace, J.; Rosowsky, A.
Structural analysis of a holoenzyme complex of mouse dihydrofolate reductase with NADPH and a ternary complex with the potent and selective inhibitor 2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine
Acta Crystallogr. Sect. D
64
977-984
2008
Pneumocystis carinii, Mus musculus (P00375), Mus musculus
Remy, I.; Campbell-Valois, F.X.; Michnick, S.W.
Detection of protein-protein interactions using a simple survival protein-fragment complementation assay based on the enzyme dihydrofolate reductase
Nat. Protoc.
2
2120-2125
2007
Mus musculus (P00375)
Ghosh, P.; Cheng, J.; Chou, T.F.; Jia, Y.; Avdulov, S.; Bitterman, P.B.; Polunovsky, V.A.; Wagner, C.R.
Expression, purification and characterization of recombinant mouse translation initiation factor eIF4E as a dihydrofolate reductase (DHFR) fusion protein
Protein Expr. Purif.
60
132-139
2008
Mus musculus
Cody, V.; Mao, Q.; Queener, S.F.
Recombinant bovine dihydrofolate reductase produced by mutagenesis and nested PCR of murine dihydrofolate reductase cDNA
Protein Expr. Purif.
62
104-110
2008
Bos taurus, Mus musculus
Gangjee, A.; Li, W.; Lin, L.; Zeng, Y.; Ihnat, M.; Warnke, L.A.; Green, D.W.; Cody, V.; Pace, J.; Queener, S.F.
Design, synthesis, and X-ray crystal structures of 2,4-diaminofuro[2,3-d]pyrimidines as multireceptor tyrosine kinase and dihydrofolate reductase inhibitors
Bioorg. Med. Chem.
17
7324-7336
2009
Homo sapiens, Mus musculus
Hughes, L.; Carton, R.; Minguzzi, S.; McEntee, G.; Deinum, E.E.; OConnell, M.J.; Parle-McDermott, A.
An active second dihydrofolate reductase enzyme is not a feature of rat and mouse, but they do have activity in their mitochondria
FEBS Lett.
589
1855-1862
2015
Homo sapiens (P00374), Homo sapiens (Q86XF0), Homo sapiens, Mus musculus (P00375), Mus musculus, Rattus norvegicus (Q920D2), Rattus norvegicus
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