A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27 .fwdarw. serine Escherichia coli dihydrofolate reductase-Reference-Cited by-同舟云学术

A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27 .fwdarw. serine Escherichia coli dihydrofolate reductase

Published:1990-09-18 Issue:37 Volume:29 Page:8561-8569
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Howell Elizabeth E.,Booth Carol,Farnum Martin,Kraut Joseph,Warren Mark S.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00489a009

Reference56 articles.

1. Evolution of enzyme function and the development of catalytic efficiency

2. Role of aspartate 27 in the binding of methotrexate to 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. Purification and properties of Escherichia coli dihydrofolate reductase

5. Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding.

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