Structure-Activity of Sulfones and Sulfonamides on Dihydropteroate Synthetase from Neisseria meningitidis

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Structure-activity of sulfones and sulfonamides on dihydropteroate synthetase from Neisseria meingitidis.

The molecular interaction of various sulfones and sulfonamides with partially purified dihydropteroate synthetase from Neisseria meningitidis M-166 has been examined. The mode of action of the sulfones was similar to that of the sulfonamides. Both groups of drugs were competitive inhibitors of dihydropteroate synthetase with respect to p-aminobenzoate in a partially purified enzyme preparation....

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Inhibition of dihydropteroate synthetase from Escherichia coli by sulfones and sulfonamides.

The inhibitory action of various diphenylsulfones and sulfonamides on dihydropteroate synthetase partially purified from Escherichia coli was examined. 4,4'-Diaminodiphenylsulfone (DDS; I(50) = 2 x 10(-5) M) and the monosubstituted derivatives 4-amino-4'-formamidodiphenylsulfone (I(50) = 5.8 x 10(-5) M) and 4-amino-4'-acetamidodiphenylsulfone (I(50) = 5.2 x 10(-5) M) were effective inhibitors o...

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Alterations in dihydropteroate synthetase in cell-free extracts of sulfanilamide-resistant Neisseria meningitidis and Neisseria gonorrhoeae.

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 K(m) for p-aminobenzoate was unaffected, the K(i) for sulfanilamide increased and the ...

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Crystal Structure of Outer Membrane Protein NMB0315 from Neisseria meningitidis

NMB0315 is an outer membrane protein of Neisseria meningitidis serogroup B (NMB) and a potential candidate for a broad-spectrum vaccine against meningococcal disease. The crystal structure of NMB0315 was solved by single-wavelength anomalous dispersion (SAD) at a resolution of 2.4 Å and revealed to be a lysostaphin-type peptidase of the M23 metallopeptidase family. The overall structure consist...

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Background: Neisseria meningitidis, a life-threatening human pathogen with the potential to cause large epidemics, can be isolated from the nasopharynx of 5–15% of adults. The aim of the current study was to evaluate biophysical and biochemical properties and immunological aspects of chimeric acyl-carrier protein-macrophage infectivity potentiator protein-type IV pilus biogenesis protein ...

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ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 1975

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.7.6.758