Interaction of the carboxamide of NADPH with Lactobacillus casei dihydrofolate reductase

Interaction of the carboxamide of NADPH with Lactobacillus casei dihydrofolate reductase

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 comple...

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Veröffentlicht in:Archives of biochemistry and biophysics 1982, Vol.213 (1), p.338-340
Hauptverfasser: Dwivedi, Chandra M., Plante, Laurence T., Kisliuk, Roy L., Pastore, Edward J., Verma, Surendra P., Wallach, Donald F.H.
Format: Artikel
Sprache:eng
Schlagworte:
Lactobacillus casei - enzymology
Methotrexate - metabolism
NADP - metabolism
Spectrum Analysis, Raman
Tetrahydrofolate Dehydrogenase - metabolism
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Zusammenfassung: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.
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(82)90471-4