A simple radioassay for dihydrofolate synthetase activity in Escherichia coli and its application to an inhibition study of new pteroate analogs

✍ Scribed by Richard I. Ho; Leonard Corman; Johnna Ho; M.G. Nair

• Publisher: Elsevier Science
• Year: 1976
• Tongue: English
• Weight: 473 KB
• Volume: 73
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(76)90199-8

✦ Synopsis

A simple radioactive assay system is elaborated for the measurement of dihydrofolate 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-IO-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.