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Interaction of the carboxamide of NADPH with Lactobacillus casei dihydrofolate reductase |
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| Authors: | Chandra M. Dwivedi Laurence T. Plante Roy L. Kisliuk Edward J. Pastore Surendra P. Verma Donald F.H. Wallach |
| Affiliation: | 1. Department of Biochemistry and Pharmacology, Tufts University School of Medicine, Boston, Massachusetts 02111 USA;2. Department of Therapeutic Radiology, Tufts-New England Medical Center, Boston, Massachusetts 02111 USA;3. Department of Chemistry, University of California, San Diego, La Jolla, California 92023 USA |
| Abstract: | Dihydrofolate reductase from Lactobacillus casei and its complexes with NADPH and methotrexate yield well-resolved Raman spectra. The 1685-cm?1 Raman band assigned to the carboxamide of NADPH persists in the NADPH-enzyme binary complex but is absent from the NADPH-methotrexate-enzyme ternary complex. This is ascribed to stabilization of the polarized form of the carboxamide by H bonding to the NH and CO groups of Ala 6 and Ile 13 of the peptide backbone. |
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