Characterization of H 2O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production

Hui Gao, Manish Kumar Tiwari, Yun Chan Kang, Jung Kul Lee

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30 Citations (Scopus)


A nicotinamide adenine dinucleotide (NADH) oxidase from Streptococcus pyogenes MGAS10394 (SpNox) was cloned and overexpressed in Escherichia coli BL21 (DE3). The purified SpNox enzyme had optimal pH and temperature of 7.0 and 55 °C, respectively, with a K m of 27.0 μM and a k cat/K m of 1.1 × 10 7 s -1 M -1. SpNox showed the highest activity among all known NADH oxidases, and site-directed mutagenesis and docking analysis shed light on the molecular basis of its unusually high activity. The characteristics of SpNox may prove to be useful for NAD + regeneration in the production of l-rare sugar.

Original languageEnglish
Pages (from-to)1931-1935
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Issue number5
Publication statusPublished - 2012 Mar 1
Externally publishedYes



  • Cofactor regeneration
  • H O-forming NADH oxidase
  • l-Rare sugar
  • Streptococcus pyogenes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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