How do mutations at phenylalanine-153 and isoleucine-155 partially suppress the effects of the aspartate-27 .fwdarw. serine mutation in Escherichia coli dihydrofolate reductase?-Reference-Cited by-同舟云学术

How do mutations at phenylalanine-153 and isoleucine-155 partially suppress the effects of the aspartate-27 .fwdarw. serine mutation in Escherichia coli dihydrofolate reductase?

Published:1993-04-01 Issue:13 Volume:32 Page:3479-3487
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dion Amanda,Linn Charles E.,Bradrick Thomas D.,Georghiou S.,Howell Elizabeth E.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00064a036

Reference65 articles.

1. Effects of distal point-site mutations on the binding and catalysis of dihydrofolate reductase from Escherichia coli

2. The function of amino acid residues contacting the nicotinamide ring of NADPH in dihydrofolate reductase from Escherichia coli

3. Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH.

4. Theoretical π-π* absorption and circular dichroic spectra of polypeptide β-structures

5. Purification and properties of Escherichia coli dihydrofolate reductase

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