Dihydropteroate synthase
Dihydropteroate synthase (pronunciation: dye-hydro-pter-o-ate synth-ase) is an enzyme that plays a crucial role in the biosynthesis of folate in bacteria. It is the target of the sulfonamide class of antibiotics, which inhibit its function and thus prevent the synthesis of folate, an essential nutrient for bacterial growth.
Etymology
The term "Dihydropteroate synthase" is derived from the chemical reaction it catalyzes. "Dihydro-" refers to the presence of two hydrogen atoms, "pteroate" refers to pteroic acid, a component of folate, and "synthase" is a class of enzymes that catalyze the formation of a compound.
Function
Dihydropteroate synthase catalyzes the condensation of para-aminobenzoic acid (PABA) and dihydropterin pyrophosphate (DHPP) to form dihydropteroate, a key intermediate in the biosynthesis of folate. This reaction is the second step in the pathway of folate synthesis and is essential for the growth and survival of many bacteria.
Clinical significance
Dihydropteroate synthase is the target of sulfonamide antibiotics. These drugs act as competitive inhibitors of the enzyme, binding to its active site and preventing the normal substrate, PABA, from binding. This inhibition disrupts the synthesis of folate and thus inhibits bacterial growth.
Related terms
- Enzyme
- Biosynthesis
- Folate
- Bacteria
- Sulfonamide
- Antibiotics
- Para-aminobenzoic acid
- Dihydropterin pyrophosphate
External links
- Medical encyclopedia article on Dihydropteroate synthase
- Wikipedia's article - Dihydropteroate synthase
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