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.
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container_end_page 340
container_issue 1
container_start_page 338
container_title Archives of biochemistry and biophysics
container_volume 213
creator Dwivedi, Chandra M.
Plante, Laurence T.
Kisliuk, Roy L.
Pastore, Edward J.
Verma, Surendra P.
Wallach, Donald F.H.
description 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.
doi_str_mv 10.1016/0003-9861(82)90471-4
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subjects Lactobacillus casei - enzymology
Methotrexate - metabolism
NADP - metabolism
Spectrum Analysis, Raman
Tetrahydrofolate Dehydrogenase - metabolism
title Interaction of the carboxamide of NADPH with Lactobacillus casei dihydrofolate reductase
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