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. 1974 Apr;5(4):388–392. doi: 10.1128/aac.5.4.388

Alterations in Dihydropteroate Synthetase in Cell-Free Extracts of Sulfanilamide-Resistant Neisseria meningitidis and Neisseria gonorrhoeae

Richard I Ho 1,2,1, Leonard Corman 1,2, Stephen A Morse 1,2, Malcolm S Artenstein 1,2
PMCID: PMC428980  PMID: 15825393

Abstract

Extracts from Neisseria meningitidis and N. gonorrhoeae with varying susceptibility to sulfanilamide have been investigated for dihydropteroate synthetase activity. Sulfanilamide was a competitive inhibitor of dihydropteroate synthetase with respect to p-aminobenzoate in extracts from both species. Though the Km for p-aminobenzoate was unaffected, the Ki for sulfanilamide increased and the Vmax decreased as the strains' resistance to sulfanilamide increased. Temperature studies have revealed differences in the dihydropteroate synthetase from N. meningitidis and N. gonorrhoeae. A direct relationship was observed between the minimal inhibitory concentration of sulfanilamide determined in vitro and the ratio of Ki/Km. This ratio may be a molecular explanation of sulfanilamide resistance for both N. meningitidis and N. gonorrhoeae.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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