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- W2010399148 abstract "Dihydrofolate reductase from strain MB 1428 of Escherichia coli was shown to catalyze the oxidative cleavage of dihydrofolate at the C(9)N(10) bond. One of the products of the reaction was identified as 7,8-dihydropterin-6-carboxaldehyde through its proton magnetic resonance spectrum. The maximal enzymatic rate was 0.05 moles dihydrofolate cleaved per minute per mole enzyme at 25° and pH 7.2, and the KM for dihydrofolate was 17.5 ± 2.5 μM. The enzymatic reaction was fully inhibitable with methotrexate. The mechanism of enzyme action was proposed to be an apparent “acidification” of dihydrofolate upon binding to the enzyme. Folate underwent an analogous oxidative cleavage by enzyme with a turnover number of 0.0014, which produced pterin-6-carboxaldehyde. Methotrexate was also slowly degraded by the enzyme." @default.
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- W2010399148 date "1973-10-01" @default.
- W2010399148 modified "2023-09-26" @default.
- W2010399148 title "Dihydrofolate reductase from a methotrexate-resistant strain of Escherichia coli: Dihydrofolate monooxygenase activity" @default.
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- W2010399148 doi "https://doi.org/10.1016/0006-291x(73)90794-8" @default.
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