A simple radioassay for dihydrofolate synthetase activity in Escherichia coli and its application to an inhibition study of new pteroate analogs |
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| Authors: | Richard I Ho Leonard Corman Johnna Ho MG Nair |
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| Institution: | 1. Samuel M. Best Research Laboratory Massachusetts College of Pharmacy, Boston, Massachusetts 02115 USA;2. Department of Biochemistry, College of Medicine, University of South Alabama, Mobile, Alabama 36688 USA |
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| Abstract: | A simple radioactive assay system is elaborated for the measurement of dihyrofolate synthetase activity in Escherichia coli. It is also applicable to Neisseria gonorrhoeae and N. meningitidis extracts. Eight oxidized and reduced pteroate analogs have been examined for inhibitory activity. The most active inhibitor was dihydrohomopteroic acid followed by dihydro-10-thiopteroic acid, dihydrofolic acid, and dihydroisopteroic acid. The enzyme appears to be incapable of binding with substrate and any of the inhibitors in their oxidized forms. |
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| Keywords: | To whom reprint requests should be addressed |
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