Dihydrofolate reductase
Dihydrofolate Reductase
Dihydrofolate reductase (pronounced: dye-hydro-fo-late re-duc-tase), often abbreviated as DHFR, is an enzyme that plays a crucial role in the synthesis of nucleotides and the metabolism of folate.
Etymology
The term "Dihydrofolate reductase" is derived from its function. "Dihydrofolate" refers to the molecule that the enzyme acts upon, and "reductase" is a type of enzyme that catalyzes reduction reactions.
Function
Dihydrofolate reductase is involved in the tetrahydrofolate synthesis pathway. It catalyzes the conversion of dihydrofolate (DHF) to tetrahydrofolate (THF). THF is a co-factor in the synthesis of purines, thymidylic acid, and certain amino acids.
Clinical Significance
Inhibitors of Dihydrofolate reductase, such as methotrexate, are used as chemotherapeutic agents in the treatment of cancer. They work by blocking the action of DHFR, thereby inhibiting DNA synthesis and cell division.
Related Terms
- Enzyme: A protein that catalyzes a specific biochemical reaction.
- Folate: A type of B vitamin that is key for cell growth and metabolism.
- Methotrexate: A chemotherapy drug and immune system suppressant.
- Tetrahydrofolate: A form of the vitamin folate that is used at the cellular level for DNA reproduction, the metabolism of amino acids, and the conversion of homocysteine to methionine.
External links
- Medical encyclopedia article on Dihydrofolate reductase
- Wikipedia's article - Dihydrofolate reductase
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