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

doi:10.1016/j.bmcl.2012.01.049

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

Research output: Contribution to journal › Article

30 Citations (Scopus)

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	https://doi.org/10.1016/j.bmcl.2012.01.049
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

Gao, H., Tiwari, M. K., Kang, Y. C., & Lee, J. K. (2012). Characterization of H ₂O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production. Bioorganic and Medicinal Chemistry Letters, 22(5), 1931-1935. https://doi.org/10.1016/j.bmcl.2012.01.049

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10.1016/j.bmcl.2012.01.049