<b>The Structure of Dihydrofolic Acid Prepared by Dithionite Reduction of Folic Acid</b>

Pastore, Edward J.; Friedkin, Morris; Jardetzky, Oleg

doi:10.1021/ja00902a066

Cited by 45 publications

(25 citation statements)

References 2 publications

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“…DPN3H was prepared by reaction of glycerol kinase and glycerol-P dehydrogenase with 3-pmoles of [2C-3H]glycerol (6 x 10' countslmin) and DPN in hydrazine (1 M) glycine (0.2 M) buffer, pH 9.8, and isolated by elution from a small column of DEAEcellulose [9]. The reaction with cc-glycerolphosphate dehydrogenase leads to a DPN3H carrying the 3H label on the side of the ring which is also attacked by glyceraldehydephosphate dehydrogenase [lo].…”

Section: Methodsmentioning

confidence: 99%

Mechanism of Ribulose-Diphosphate Carboxydismutase Reaction

et al. 1967

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Ribulose-1 ,5-P, labelled with tritium in the C-3 position was converted to 2 moles of phosphoglyceric acid by the carboxydismutase. Over 98 Olio of the radioactivity was found in the water, less than 0.1 being in phosphoglyceric acid, indicating that the proton lost from the 3 position of the substrate does not contribute to the formation of product. The tritiated substrate reacts a t only 200/0 the rate of the normal carrier species. Neither substrate nor product show significant proton exchange with the medium due to the enzyme.

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Section: Methodsmentioning

confidence: 99%

Mechanism of Ribulose-Diphosphate Carboxydismutase Reaction

et al. 1967

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“…These principles are now being applied profitably to studies on a wide range of less well-characterized biologically important proteins (4). As an extension of our earlier proton magnetic resonance (PMR) studies of folate coenzymes (5,6) (9,10) and an effective affinity column purification procedure (11). While low molecular weight enzymes have been examined successfully by NMR spectroscopy during the past several years (2,3) …”

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confidence: 94%

Conformational Changes Induced in Dihydrofolate Reductase by Folates, Pyridine Nucleotide Coenzymes, and Methotrexate

Pastore¹,

Kisliuk

Plante³

et al. 1974

Proc. Natl. Acad. Sci. U.S.A.

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“…On the other hand, the E. coli DHFR was considerably more specific in-its requirement for the adeno- (29)(30)(31)(32)(33). Similarly, about 1 mol of tetrahydrofolate was produced per mol of dihydrofolate consumed when a-NADPH was the substrate.…”

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confidence: 99%

Alpha-pyridine nucleotides as substrates for a plasmid-specified dihydrofolate reductase.

Smith¹,

Burchall²

1983

Proc. Natl. Acad. Sci. U.S.A.

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The a epimers of pyridine nucleotides are almost totally inactive as reductants in dehydrogenase reactions. In contrast, the R plasmid R67-specified dihydrofolate reductase (5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) isolated from trimethoprim-resistant Escherichia coli utilized a-NADPH and a-NADH in addition to the "normal" 3-epimers. The enzymes from bacterial and mammalian sources used only 13-NADPH and ,B-NADH. The K. value for ax-NADPH (16 ,uM) was 4-fold greater than that for .8-NADPH (4 ,AM), while the maximal velocity of the a-NADPH-catalyzed reaction was 70% of that seen with the .3-NADPH. P-NADP+ and a-NADP+ were competitive inhibitors of the R67 enzyme. Pyridine nucleotide analogues such as deamino-and acetyl-NADPH were used readily by bacterial, plasmid, and mammalian enzymes, whereas thio-NADPH was used only by the plasmid enzyme. These data suggest that the enzyme from R plasmid R67 possesses a pyridine nucleotide binding site different from that of other dihydrofolate reductases and dehydrogenases.

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The Structure of Dihydrofolic Acid Prepared by Dithionite Reduction of Folic Acid

Cited by 45 publications

References 2 publications

Mechanism of Ribulose-Diphosphate Carboxydismutase Reaction

Mechanism of Ribulose-Diphosphate Carboxydismutase Reaction

Conformational Changes Induced in Dihydrofolate Reductase by Folates, Pyridine Nucleotide Coenzymes, and Methotrexate

Alpha-pyridine nucleotides as substrates for a plasmid-specified dihydrofolate reductase.

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