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• W258206170 abstract "The state of protonation of substrates bound to mammalian dihydrofolate reductase (DHFR) has significance for the mechanism of catalysis. To investigate this, dihydrofolate and dihydropteroyl-pentaglutamate have been synthesized with 15N enrichment at N-2. 15N NMR studies have been performed on the binary complexes formed by bovine DHFR with these compounds and with [5-15N]dihydrobiopterin. The results indicate that there is no protonation at N-5 in the binary complexes, and this was confirmed by 13C NMR studies with folate and dihydrofolate synthesized with 13C enrichment at C-6. The chemical shift displacements produced by complex formation are in the same direction as those which result from deprotonation of the N-3/C-4-O amide group and are consistent with at least partial loss of the proton from N-3. This would be possible if, as crystallographic data indicate, there is interaction of N-3 and the 2-amino group of the bound ligands with the carboxylate of the active site glutamate residue (Glu30)." @default.
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• W258206170 date "1990-02-06" @default.
• W258206170 modified "2023-09-25" @default.
• W258206170 title "Carbon-13 and nitrogen-15 nuclear magnetic resonance evidence of the ionization state of substrates bound to bovine dihydrofolate reductase" @default.
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• W258206170 doi "https://doi.org/10.1021/bi00457a026" @default.
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