A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27 .fwdarw. serine Escherichia coli dihydrofolate reductase
- 18 September 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (37) , 8561-8569
- https://doi.org/10.1021/bi00489a009
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 3 references indexed in Scilit:
- Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH.Journal of Biological Chemistry, 1990
- Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substratesBiochemistry, 1988
- Interpreting the Behavior of Enzymes Purpose or Pedigree?Critical Reviews in Biochemistry, 1988