Skip to main content

Substrate and inhibitor binding to dihydrofolate reductase

  • Chapter

Part of the book series: Biological Council ((BCSDA))

Abstract

Dihydrofolate reductase (5, 6, 7, 8-tetrahydrofolate:NADP+ oxidoreductase, E.C.1.5.1.3), an enzyme found in the vast majority of both prokaryotic and eukaryotic organisms, catalyses the reduction of dihydrofolate to tetrahydrofolate, using NADPH as coenzyme:

The product of this reaction, tetrahydrofolate, plays a vital role in intermediary metabolism, acting as a ‘carrier’ of one-carbon fragments in the biosynthesis of a number of amino acids, thymidylate and purines (for a review, see Blakley, 1969).

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   44.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   59.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Copyright information

© 1977 Institute of Biology Endowment Trust Fund

About this chapter

Cite this chapter

Roberts, G.C.K. (1977). Substrate and inhibitor binding to dihydrofolate reductase. In: Roberts, G.C.K. (eds) Drug Action at the Molecular Level. Biological Council. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-03230-3_7

Download citation

Publish with us

Policies and ethics