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• W1596727844 abstract "Interaction of several representative folate, quinazoline and pyridine nucleotide derivatives with dihydrofolate reductase from amethopterin-resistant Lactobacillus casei induces dramatic changes in its circular dichroic spectral properties. The binding of dihydrofolate induces a large extrinsic Cotton effect at 295 nm ([theta] = 113 800 deg . cm2 . dm-1). The generation of this band by dihydrofolate is strictly dependent on complex formation with a single substrate binding site and a KD = 7 . 10(-6) M. The other binary complexes examined include the enzyme . NADPH, enzyme . amethopterin, enzyme . folate, and enzyme . methasquin. All such complexes differ in spectral detail, the negative ellipticity at 330 nm being characteristic of the folate site complexes. The circular dichroic spectrum of the ternary complex of reductase . NADPH . methotrexate shows a positive symmetrical band centered at 360 nm ([theta] - 32 000 deg . cm2 . dm-1). Since both of the corresponding binary complexes exhibit negative bands in this region, this induced band represents a unique molecular property of the ternary complex. Chemical modification of a single tryptophan residue of the enzyme, as determined from magnetic circular dichroism spectra, results in a complete loss in the ability to bind either dihydrofolate or NADPH." @default.
• W1596727844 created "2016-06-24" @default.
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• W1596727844 date "1978-04-01" @default.
• W1596727844 modified "2023-09-23" @default.
• W1596727844 title "Binary and ternary complexes of dihydrofolate reductase with substrates, coenzymes and inhibitors" @default.
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• W1596727844 doi "https://doi.org/10.1016/0005-2795(78)90387-2" @default.
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