Direct experimental evidence for competitive inhibition of dihydrofolate reductase by methotrexate

Mark C. Waltham, John W. Holland, Scott C. Robinson, Donald J. Winzor, Peter F. Nixon

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Steady-state enzyme kinetic techniques at very low enzyme concentration (0.4 nM) were used successfully to measure the inhibition constant (53 pM) for the dissociation of methotrexate from the ternary complex of methotrexate, NADPH and dihydrofolate reductase from Lactobacillus casei; and to demonstrate unequivocally that the inhibition was, indeed, competitive with respect to dihydrofolate.

Original languageEnglish
Pages (from-to)535-539
Number of pages5
JournalBiochemical Pharmacology
Issue number3
Publication statusPublished - 1 Feb 1988
Externally publishedYes

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