Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration.

Biochemistry
Yaozhong ZouSatish K Nair

Abstract

The enzyme phosphite dehydrogenase (PTDH) catalyzes the NAD(+)-dependent conversion of phosphite to phosphate and represents the first biological catalyst that has been shown to conduct the enzymatic oxidation of phosphorus. Despite investigation for more than a decade into both the mechanism of its unusual reaction and its utility in cofactor regeneration, there has been a lack of any structural data for PTDH. Here we present the cocrystal structure of an engineered thermostable variant of PTDH bound to NAD(+) (1.7 Å resolution), as well as four other cocrystal structures of thermostable PTDH and its variants with different ligands (all between 1.85 and 2.3 Å resolution). These structures provide a molecular framework for understanding prior mutational analysis and point to additional residues, located in the active site, that may contribute to the enzymatic activity of this highly unusual catalyst.

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Citations

May 6, 2014·Trends in Biotechnology·Xiulai ChenLiming Liu
Oct 28, 2016·Chemical Reviews·Geoff P Horsman, David L Zechel
Mar 28, 2018·Journal of Industrial Microbiology & Biotechnology·Jiaheng LiuJianjun Qiao
Sep 11, 2019·Biotechnology and Bioengineering·Xiao-Yang OuWen-Yong Lou
Jan 27, 2021·Chemistry : a European Journal·Christian SchnepelNorbert Sewald
Dec 12, 2018·Journal of the American Chemical Society·Graeme W Howe, Wilfred A van der Donk
Jul 13, 2019·Journal of the American Chemical Society·Jin GuoKatherine S Ryan

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