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Article

Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase.

The Journal of biological chemistry - 12 May 2006

Iwakura Masahiro, Maki Kosuke, Takahashi Hisashi, Takenawa Tatsuyuki, Yokota Akiko, Katayanagi Katsuo, Kamiyama Tadashi, Gekko Kunihiko

Abstract excerpt

We developed a strategy for finding out the adapted variants of enzymes, and we applied it to an enzyme, dihydrofolate reductase (DHFR), in terms of its catalytic activity so that we successfully obtained several hyperactive cysteine- and methionine-free variants of DHFR in which all five methionyl and two cysteinyl residues were replaced by other amino acid residues. Among them, a variant...

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Source

Identifiers

PMID: 16510443
DOI: 10.1074/jbc.M508823200

Genes

DHFR

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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