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Article

Molecular basis for nonadditive mutational effects in Escherichia coli dihydrofolate reductase.

Biochemistry - 5 Dec 1995

Wagner C R, Huang Z, Singleton S F, Benkovic S J

Abstract excerpt

Recently, two sets of single, double, and quadruple residue changes within the hydrophobic substrate binding pocket of Escherichia coli dihydrofolate reductase (5,6,7,8-tetrahydrofolate+ oxidoreductase, EC 1.5.1.3) were shown to exhibit nonadditive mutational effects [Huang, Z., Wagner, C. R., & Benkovic, S. J. (1994) Biochemistry 33, 11576--11585]. In particular, the analysis of data for the L28Y, L54F, and...

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PMID: 7495797
DOI: 10.1021/bi00048a011

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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