Stretching exercises - Flexibility in dihydrofolate reductase catalysis

Grover Paul Miller, Stephen Benkovic

Research output: Contribution to journalReview article

93 Citations (Scopus)

Abstract

As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis. Studies discussed in this review highlight the role of conformational flexibility in both of these enzymatic functions.

Original languageEnglish (US)
JournalChemistry and Biology
Volume5
Issue number5
DOIs
StatePublished - Jan 1 1998

Fingerprint

Tetrahydrofolate Dehydrogenase
Coenzymes
Catalysis
NADP
Folic Acid
Stretching
Regeneration
Enzymes
Substrates
5,6,7,8-tetrahydrofolic acid
dihydrofolate

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

Cite this

Miller, Grover Paul ; Benkovic, Stephen. / Stretching exercises - Flexibility in dihydrofolate reductase catalysis. In: Chemistry and Biology. 1998 ; Vol. 5, No. 5.
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Stretching exercises - Flexibility in dihydrofolate reductase catalysis. / Miller, Grover Paul; Benkovic, Stephen.

In: Chemistry and Biology, Vol. 5, No. 5, 01.01.1998.

Research output: Contribution to journalReview article

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