Abstract
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 language | English |
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Pages (from-to) | 1931-1935 |
Number of pages | 5 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 22 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2012 Mar 1 |
Externally published | Yes |
Keywords
- Cofactor regeneration
- H O-forming NADH oxidase
- Streptococcus pyogenes
- l-Rare sugar
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry