2.5.1.15	drug target	dihydropteroate synthase is the target of the sulfonamide class of drugs	759244	
2.5.1.15	drug target	drug-resistant strains of Helicobacter pylori and multitudinous drug reactions are obstacles in the treatment of Helicobacter pylori infections a reliable tertiary structure of dihydropteroate synthase in complex with inhibitor 4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide is constructed by Modeler 9v19. DrugBank compounds of DHPS, published inhibitors, and co-crystal ligand (4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide) are docked against dihydropteroate synthase. The best docked compounds are screened against 28.5 million compounds result 1186 structural analogs. Virtual screening workflow and quantum polarized ligand dockings of these compounds against dihydropteroate synthase result three leads that show better XP Gscores, ADME properties, and binding-free energies compared to 4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide, DrugBank compounds, and published inhibitors. The proposed leads are also validated by receiver operative characteristic (ROC) curve metrics in the presence of thousand decoys and the best docked existing compounds against DHPS. Long-range molecular dynamics (MD) simulations for 100 ns are executed after post-docking evaluations. Trajectory analysis shows that inter-molecular interactions of the lead-dihydropteroate synthase docking complex are stable throughout the entire runtime of MD simulations than 6MB-DHPS complex and Eliglustat-DHPS complex. The study outcomes show good competitive binding propensity and active-tunneling of leads over the existing inhibitors, thereby these leads could be ideal inhibitors against dihydropteroate synthase to target Helicobacter pylori	-, 759674	
2.5.1.15	drug target	target for anti-malarial and anti-bacterial drugs	759889	
2.5.1.15	drug target	the enzyme is a sulfa drug target in malaria treatment	758651	
2.5.1.15	drug target	the enzyme is target of drugs like sulfadoxine (SDX). The SDX effectiveness as an antimalarial drug is increasingly diminished by the rise and spread of drug-resistant mutations	-, 759490	
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	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	metabolism	dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes	723771	
2.5.1.15	metabolism	reactions in the folate biosynthetic pathway	-, 759490	
2.5.1.15	metabolism	the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis	-, 759674	
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	additional information	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	additional information	the 4-amino benzoic acid/sulfonamide binding site is formed close to the protein surface by flexible protein loops	721829	
2.5.1.15	additional information	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	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	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