Inhibition of dihydrofolate reductase from bacterial and vertebrate sources by folate, aminopterin, methotrexate and their 5-deaza analogues.

@article{Stone1984InhibitionOD,
  title={Inhibition of dihydrofolate reductase from bacterial and vertebrate sources by folate, aminopterin, methotrexate and their 5-deaza analogues.},
  author={S. Stone and J. Montgomery and J. F. Morrison},
  journal={Biochemical pharmacology},
  year={1984},
  volume={33 2},
  pages={
          175-9
        }
}
  • S. Stone, J. Montgomery, J. F. Morrison
  • Published 1984
  • Biology, Medicine
  • Biochemical pharmacology
    • The inhibition of dihydrofolate reductases from Escherichia coli and chicken liver by folate, methotrexate, aminopterin and their 5-deaza analogues was investigated to examine the importance of the N-5 nitrogen in slow-binding inhibition. Methotrexate, aminopterin and their 5-deaza analogues acted as slow, tight-binding inhibitors of both enzymes. Inhibition by methotrexate and 5-deazamethotrexate conformed to a mechanism in which there is an initial rapid formation of an enzyme-NADPH-inhibitor… CONTINUE READING
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    37 Citations
    Background Citations
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    Methods Citations
    1
    Results Citations
    1
    37 Citations
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    Synthesis and biological evaluation of a fluorescent analogue of folic acid.
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    Monitoring the effect of triamterene and hydrochlorothiazide on dihydrofolate reductase activity using a new spectrophotometric method.
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    Assessment of methotrexate on dihydrofolate reductase activity, total RNA content and cell division of Lathyrus sativus L.
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