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Information on EC 1.5.1.3 - dihydrofolate reductase and Organism(s) Drosophila melanogaster and UniProt Accession P17719

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EC Tree
     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.3 dihydrofolate reductase
IUBMB Comments
The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: P17719
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The taxonomic range for the selected organisms is: Drosophila melanogaster
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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 hide
9002-03-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydrofolate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
show the reaction diagram
-
-
-
?
7,8-dihydrofolate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
show the reaction diagram
-
strongly specific for
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
show the reaction diagram
-
no activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methotrexate
wild-type, 50% inhibition at 1.06 nM, mutant Q134K, 50% inhibition at 16.7 nM, mutant L30Q, 50% inhibition at 785 nM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004 - 0.00592
7,8-dihydrofolate
0.0055 - 0.0071
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
2 optima: pH 4.7 and pH 8.5
8.5
-
2 optima: pH 4.7 and pH 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression in Chinese hamster ovary cells
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DYR_DROME
182
0
20775
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 17000-22000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I26N/K31P
less than 10% of wild-type activity
K31P
no detectable activity
L22R
mutation predicted in silico to be resistant to methotrexate, confers resistance to methotrexate to transfected CHO cells. 65% of wild-type enzyme activity
L30Q
mutation found in a methotrexate resistant cell line, confers resistance to methotrexate to transfected CHO cells. 42% of wild-type enzyme activity
Q134K
51% of wild-type enzyme activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized by 0.1 mg/ml bovine serum albumin and 1 mM dithiothreitol at 4°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
on ice, loss of 20-60% activity after 2 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rancourt, S.L.; Walker, V.K.
The purification of dihydrofolate reductase from Drosophila melanogaster
Biochim. Biophys. Acta
1039
261-268
1990
Drosophila melanogaster
Manually annotated by BRENDA team
Walker, V.K.; Tyshenko, M.G.; Kuiper, M.J.; Dargar, R.V.; Yuhas, D.A.; Cruickshank, P.A.; Chaguturu, R.
Tobacco budworm dihydrofolate reductase is a promising target for insecticide discovery
Eur. J. Biochem.
267
394-402
2000
Drosophila melanogaster, Heliothis virescens
Manually annotated by BRENDA team
Affleck, J.G.; Al-Batayneh, K.M.; Neumann, K.; Cole, S.P.; Walker, V.K.
Drosophila dihydrofolate reductase mutations confer antifolate resistance to mammalian cells
Eur. J. Pharmacol.
529
71-78
2006
Drosophila melanogaster (P17719)
Manually annotated by BRENDA team