Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase

A Achari, DO Somers, JN Champness… - Nature structural …, 1997 - nature.com
Sulfonamides were amongst the first clinically useful antibacterial agents to be discovered.
The identification of sulfanilamide as the active component of the dye Prontosil rubrum led to …

Crystal structure of 7, 8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design

K Babaoglu, J Qi, RE Lee, SW White - Structure, 2004 - cell.com
Dihydropterate synthase (DHPS) is the target for the sulfonamide class of antibiotics, but
increasing resistance has encouraged the development of new therapeutic agents against …

Catalysis and sulfa drug resistance in dihydropteroate synthase

MK Yun, Y Wu, Z Li, Y Zhao, MB Waddell, AM Ferreira… - Science, 2012 - science.org
The sulfonamide antibiotics inhibit dihydropteroate synthase (DHPS), a key enzyme in the
folate pathway of bacteria and primitive eukaryotes. However, resistance mutations have …

Structural studies of pterin-based inhibitors of dihydropteroate synthase

KE Hevener, MK Yun, J Qi, ID Kerr… - Journal of medicinal …, 2010 - ACS Publications
Dihydropteroate synthase (DHPS) is a key enzyme in bacterial folate synthesis and the
target of the sulfonamide class of antibacterials. Resistance and toxicities associated with …

Crystal structure of Mycobacterium tuberculosis 6-hydroxymethyl-7, 8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic …

AM Baca, R Sirawaraporn, S Turley… - Journal of molecular …, 2000 - Elsevier
The enzyme 6-hydroxymethyl-7, 8-dihydropteroate synthase (DHPS) catalyzes the
condensation of para-aminobenzoic acid (pABA) with 6-hydroxymethyl-7, 8-dihydropterin …

Molecular mechanism of plasmid-borne resistance to sulfonamide antibiotics

M Venkatesan, M Fruci, LA Verellen, T Skarina… - Nature …, 2023 - nature.com
The sulfonamides (sulfas) are the oldest class of antibacterial drugs and inhibit the bacterial
dihydropteroate synthase (DHPS, encoded by folP), through chemical mimicry of its co …

The Structural and Functional Basis for Recurring Sulfa Drug Resistance Mutations in Staphylococcus aureus Dihydropteroate Synthase

EC Griffith, MJ Wallace, Y Wu, G Kumar… - Frontiers in …, 2018 - frontiersin.org
Staphylococcal species are a leading cause of bacterial drug-resistant infections and
associated mortality. One strategy to combat bacterial drug resistance is to revisit …

Structure and function of the dihydropteroate synthase from Staphylococcus aureus

IC Hampele, A D'Arcy, GE Dale, D Kostrewa… - Journal of molecular …, 1997 - Elsevier
The gene encoding the dihydropteroate synthase of staphylococcus aureus has been
cloned, sequenced and expressed in Escherichia coli. The protein has been purified for …

Origin of the mobile di-hydro-pteroate synthase gene determining sulfonamide resistance in clinical isolates

M Sánchez-Osuna, P Cortés, J Barbé… - Frontiers in microbiology, 2019 - frontiersin.org
Sulfonamides are synthetic chemotherapeutic agents that work as competitive inhibitors of
the di-hydro-pteroate synthase (DHPS) enzyme, encoded by the folP gene. Resistance to …

Replacing sulfa drugs with novel DHPS inhibitors

DI Hammoudeh, Y Zhao, SW White… - Future medicinal …, 2013 - Taylor & Francis
More research effort needs to be invested in antimicrobial drug development to address the
increasing threat of multidrug-resistant organisms. The enzyme DHPS has been a validated …