Dihydrofolate reductase

Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as an electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q14.1 region of chromosome 5.

DHFR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDHFR, DHFRP1, DYR, dihydrofolate reductase
External IDsOMIM: 126060 MGI: 94890 HomoloGene: 56470 GeneCards: DHFR
Orthologs
SpeciesHumanMouse
Entrez

1719

13361

Ensembl

ENSG00000228716

ENSMUSG00000021707

UniProt

P00374

P00375

RefSeq (mRNA)

NM_000791
NM_001290354
NM_001290357

NM_010049

RefSeq (protein)

NP_000782
NP_001277283
NP_001277286

NP_034179

Location (UCSC)Chr 5: 80.63 – 80.65 MbChr 13: 92.49 – 92.53 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

There are two structural classes of DHFR, evolutionarily unrelated to each other. The former is usually just called DHFR and is found in bacterial chromosomes and animals. In bacteria, however, antibiotic pressure has caused this class to evolve different patterns of binding diaminoheterocyclic molecules, leading to many "types" named under this class, while mammalian ones remain highly similar. The latter (type II), represented by the plastid-encoded R67, is a tiny enzyme that works by forming a homotetramer.

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