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Title 

Role of surface residue 184 in the catalytic activity of NADH oxidase from Streptococcus pyogenes

 

Streptococcus pyogenes 내 NADH oxidase의 활성에 있어 184번 아미노산의 역할

Authors 

H GaoM K TiwariR K SinghBong Hyun SungS C KimJ K Lee

Publisher 

Springer Verlag (Germany)

Issue Date 

2014

Citation 

Applied Microbiology and Biotechnology, vol. 98, no. 16, pp. 7081-7088

Keywords 

Catalytic efficiencyl-Rare sugarSite-directed mutagenesis

Abstract 

Nicotinamide adenine dinucleotide (NADH) oxidase from Streptococcus pyogenes (SpNox) is a flavoprotein harboring one molecule of noncovalently bound flavin adenine dinucleotide. It catalyzes the oxidation of NADH by reducing molecular O2 to H2O directly through a four-electron reduction. In this study, we selected the lysine residues on the surface of SpNox and mutated them into arginine residues to study the effect on the enzyme activity. A single-point mutation (K184R) at the surface of SpNox enhanced NADH oxidase activity by approximately 50 % and improved thermostability with 46.6 % longer half life at 30°C. Further insights into the function of residue K184 were obtained by substituting it with other nonpolar, polar, positively charged, and negatively charged residues. To elucidate the role of this residue, computer-assisted molecular modeling and substrate docking were performed. The results demonstrate that even a single mutation at the surface of the enzyme induces changes in the interaction at the active site and affects the activity and stability. Additionally, the data also suggest that the K184R mutant can be used as an effective biocatalyst for NAD+ regeneration in L-rare sugar production.

ISSN 

0175-7598

Link 

http://dx.doi.org/10.1007/s00253-014-5666-y

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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