ScienceAsia 10 (1984): 135-145 |doi: 10.2306/scienceasia1513-1874.1984.10.135

INHIBITION OF DIHYDROPTEROA TE SYNTHASE FROM ESCHERICHIA COLI BY FIVE SULFONAMIDES

NAPAPORN SAI-UBOL^a and WICHAI SUTTIMOOL^b

ABSTRACT: The inhibitory action of five sulfonamides on dihydropteroate synthase purified from Escherichia coli was studied. The inhibitor constants (K) for sulfanilamide, 3-(4-aminophenylsulfonamido) propyl bromide, N, N'-bis(sulfanilyl)-L-cystine, sodium 3-(4- aminophenylsulfonamido) propanethiosulfate and N-[4-(4-aminophenylsulfonamido) phenylsulfonylj glycine were 4.30 X 10^-4, 7.50 X 10^-4, 3.50 X 10^-4, 5.38 X 10^-4 and 7.50 X 10^-6 M respectively. All five sulfonamides showed their inhibitory activity by competing with p-aminobenzoic acid for the active site of dihydropteroate synthase,

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a. Department of Immunology and Biochemistry, Armed Forces Research Institute of Medical-Sciences, Bangkok, Thailand.
b. Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand.

Received 28 May 1984