Title : NMR studies of the interaction of a type II dihydrofolate reductase with pyridine nucleotides reveal unexpected phosphatase and reductase activity.

Pub. Date : 2003 Sep 30

PMID : 14503865






5 Functional Relationships(s)
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1 The interaction of type II R67 dihydrofolate reductase (DHFR) with its cofactor nicotinamide adenine dinucleotide phosphate (NADP(+)) has been studied using nuclear magnetic resonance (NMR). NADP dihydrofolate reductase Escherichia coli
2 The interaction of type II R67 dihydrofolate reductase (DHFR) with its cofactor nicotinamide adenine dinucleotide phosphate (NADP(+)) has been studied using nuclear magnetic resonance (NMR). NADP dihydrofolate reductase Escherichia coli
3 The degeneracy of the amide (1)H and (15)N shifts of the tetrameric DHFR was preserved upon addition of NADP(+), consistent with kinetic averaging among equivalent binding sites. NADP dihydrofolate reductase Escherichia coli
4 Analysis of the more titration-sensitive DHFR amide resonances as a function of added NADP(+) gave a K(D) of 131 +/- 50 microM, consistent with previous determinations using other methodology. NADP dihydrofolate reductase Escherichia coli
5 We have found that the (1)H spectrum of NADP(+) in the presence of the R67 DHFR changes as a function of time. NADP dihydrofolate reductase Escherichia coli