title: Stretching exercises--flexibility in dihydrofolate reductase catalysis.
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.
authors.affiliation: Department of Chemistry, Pennsylvania State University, University Park 16802, USA.
authors.forename: G P
authors.initials: GP
authors.lastname: Miller
authors.forename: S J
authors.initials: SJ
authors.lastname: Benkovic
mesh_terms: D002384:Catalysis; D018360:Crystallography, X-Ray; D008024:Ligands; D011487:Protein Conformation; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008024:Ligands; D013762:Tetrahydrofolate Dehydrogenase