EC Number   |
General Information |
Reference  |
|---|
    2.5.1.15 | malfunction |
prevalence and frequency of the dihydropteroate synthetase mutations associated with sulfadoxine-pyrimethamine resistance in southern Mozambique are examined between 1999 and 2004. The dihydropteroate synthetase double mutation frequency peaks in 2001 but declines to baseline levels by 2004. Parasites with both dihydrofolate reductase triple and dihydropteroate synthetase double mutations increase in 2001 but decrease by 2004. The peaking of sulfadoxine-pyrimethamine resistance markers in 2001 coincides with a sulfadoxine-pyrimethamine-resistant malaria epidemic in neighboring KwaZulu-Natal, South Africa. The decline in dihydropteroate synthetase (but not dihydrofolate reductase) mutations correspond with replacement of sulfadoxine-pyrimethamine with artemether-lumefantrine as malaria treatment policy in KwaZulu-Natal |
684380 |
| 2.5.1.15 | physiological function |
the prevalence of DHPS mutations in Pneumocystis jirovecii strains isolated from South African Pneumocystis jirovecii pneumonia patients are examined. Mutations resulting in amino-acid substitutions Thr55Ala and/or Pro57Ser are detected in Pneumocystis jirovecii from 85/151 (56%) patients. The high frequency of PCP episodes with Pneumocystis jirovecii harbouring DHPS mutations in South Africa indicates that populations of this fungus are evolving under considerable selective pressure exerted by sulfa-containing antibiotics |
702229 |
| 2.5.1.15 | physiological function |
mutation at DHPS locus amongst Pneumocystis jiroveci isolates obtained at a tertiary care hospital in north India are investigated. Using microscopic examination Pneumocystis jiroveci is detected in four cases and major surface glycoprotein gene is amplified in five cases. Further, amplification of DHPS gene is successful in four of the five cases positive by major surface glycoprotein gene PCR. No point mutation is observed and all four isolates presented wild-type sequences at DHPS gene by RFLP analysis |
703994 |
| 2.5.1.15 | more |
the 4-amino benzoic acid/sulfonamide binding site is formed close to the protein surface by flexible protein loops |
721829 |
| 2.5.1.15 | metabolism |
the enzyme supports the biosynthesis of folate, a key metabolite required to support the synthesis of DNA, and proteins |
721948 |
| 2.5.1.15 | more |
analysis of DHPS active site and interactions with the enzyme product 7,8-dihydropteroate, overview. DHPS shows plasticity near the substrate-binding pocket and a range of loop conformations that contribute to the architecture of the DHPS active site |
721948 |
| 2.5.1.15 | more |
the enzyme is bifunctional exhibiting 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK, EC 2.7.6.3, and dihydropteroate synthase, DHPS, activities, that catalyze sequential metabolic reactions in the folate biosynthetic pathway of bacteria and lower eukaryotes, structural organization between FtHPPK and FtDHPS which are tethered together by a short linker, overview. Each active site binds substrate in the same manner observed in the monofunctional forms. Structures of the active site loops in the DHPS module |
723522 |
| 2.5.1.15 | evolution |
dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes |
723771 |
| 2.5.1.15 | metabolism |
dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes |
723771 |
| 2.5.1.15 | drug target |
the enzyme is a sulfa drug target in malaria treatment |
758651 |
