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Dihydropteroate synthase (Escherichia coli, strain K12) (None)
- Target
- None
- Molecular classification
- Enzyme, TIM-barrel protein
01
Overview
Dihydropteroate synthase (DHPS; EC 2.5.1.15) is a key enzyme in the folate biosynthesis pathway of bacteria, including *Escherichia coli* (strain K12). It catalyzes the condensation of 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPPP) with para-aminobenzoic acid (pABA) to form 7,8-dihydropteroate and pyrophosphate. DHPS is essential for de novo folate synthesis and is targeted by sulfonamide antibiotics. Resistance to sulfonamides is a major clinical concern.
- Other names
- DHPSDihydropteroate synthetaseEC 2.5.1.15
02
Mechanism of action
Competitive inhibition of pABA binding site, blocking folate synthesis.
03
Biological functions
Folate biosynthesisBacterial growth
04
Disease associations
Infection
05
Safety considerations
Antibiotic resistancePoint mutations conferring resistanceHorizontal gene transfer of resistant alleles
06
Interacting drugs
Sulfonamides
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