EC 1 - Oxidoreductases
EC 1.5 - Acting on the CH-NH group of donors
EC 1.5.1 - With NAD+ or NADP+ as acceptor
EC 1.5.1.3 - Dihydrofolate reductase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.5.1.3
Names
Accepted name:
dihydrofolate reductase
Other
names:
7,8-dihydrofolate reductase
DHFR
NADPH-dihydrofolate reductase
dihydrofolate reductase:thymidylate synthase
dihydrofolic acid reductase
dihydrofolic reductase
folic acid reductase
folic reductase
pteridine reductase:dihydrofolate reductase
tetrahydrofolate dehydrogenase
thymidylate synthetase-dihydrofolate reductase
DHFR
NADPH-dihydrofolate reductase
dihydrofolate reductase:thymidylate synthase
dihydrofolic acid reductase
dihydrofolic reductase
folic acid reductase
folic reductase
pteridine reductase:dihydrofolate reductase
tetrahydrofolate dehydrogenase
thymidylate synthetase-dihydrofolate reductase
Systematic name:
5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase
Reaction
- 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
Comments:
The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00072
Gene Ontology:
GO:0004146
CAS Registry Number:
9002-03-3
References
-
Dihydrofolic reductase from Streptococcus faecalis R.J. Biol. Chem. 236 : 1163 (1961).
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Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate.J. Biol. Chem. 257 : 13650-13662 (1982). [PMID: 6815178]
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Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver.J. Biol. Chem. 241 : 1319-1328 (1966). [PMID: 4379915]
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Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli.Biochim. Biophys. Acta 177 : 401-411 (1969). [PMID: 4306838]
[EC 1.5.1.3 created 1961, modified 1976 (EC 1.5.1.4 created 1961, incorporated 1976)]