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Article

Reactivity of asparagine residue at the active site of the D105N mutant of fluoroacetate dehalogenase from Moraxella sp. B.

Biochimica et biophysica acta - 8 Apr 2004

Ichiyama Susumu, Kurihara Tatsuo, Kogure Yoshifumi, Tsunasawa Susumu, Kawasaki Haruhiko, Esaki Nobuyoshi

Abstract excerpt

Fluoroacetate dehalogenase from Moraxella sp. B (FAc-DEX) catalyzes cleavage of the carbon-fluorine bond of fluoroacetate, whose dissociation energy is among the highest found in natural products. Asp105 functions as the catalytic nucleophile that attacks the alpha-carbon atom of the substrate to displace the fluorine atom. In spite of the essential role of Asp105, we found that site-directed mutagenesis to...

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PMID: 15063312
DOI: 10.1016/j.bbapap.2003.10.002

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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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