A highly specific glyoxylate reductase derived from a formate dehydrogenase.

doi:10.1016/j.bbrc.2007.02.027

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Article

A highly specific glyoxylate reductase derived from a formate dehydrogenase.

Biochemical and biophysical research communications - 13 Apr 2007

Shinoda Takeshi, Arai Kazuhito, Taguchi Hayao

Abstract excerpt

A Glu141Asn mutant Paracoccus sp. 12-A formate dehydrogenase catalyzes marked glyoxylate reduction. Additional replacement of the His332-Gln313 pair with His-Glu, which is a consensus acid/base catalyst in D-hydroxyacid dehydrogenases, further improved the catalytic activity of the enzyme as to glyoxylate reduction through enhancement of the hydrogen transfer step in the catalytic process, slightly shifting the...

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Share to Alcohol Oxidoreductases
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Share to Hydrogen-Ion Concentration
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Identifiers

PMID: 17320818
DOI: 10.1016/j.bbrc.2007.02.027

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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