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 |
|---|---|
| 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 |
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Keywords
- 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
Cite this
Characterization of H 2O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production. / Gao, Hui; Tiwari, Manish Kumar; Kang, Yun Chan; Lee, Jung Kul.
In: Bioorganic and Medicinal Chemistry Letters, Vol. 22, No. 5, 01.03.2012, p. 1931-1935.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of H 2O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production
AU - Gao, Hui
AU - Tiwari, Manish Kumar
AU - Kang, Yun Chan
AU - Lee, Jung Kul
PY - 2012/3/1
Y1 - 2012/3/1
N2 - 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.
AB - 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.
KW - Cofactor regeneration
KW - H O-forming NADH oxidase
KW - l-Rare sugar
KW - Streptococcus pyogenes
UR - http://www.scopus.com/inward/record.url?scp=84857367018&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84857367018&partnerID=8YFLogxK
U2 - 10.1016/j.bmcl.2012.01.049
DO - 10.1016/j.bmcl.2012.01.049
M3 - Article
VL - 22
SP - 1931
EP - 1935
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
SN - 0960-894X
IS - 5
ER -