Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration

Yaozhong Zou, Houjin Zhang, Joseph S. Brunzelle, Tyler W. Johannes, Ryan Woodyer, John E. Hung, Nikhil Nair, Wilfred A. Van Der Donk, Huimin Zhao, Satish K. Nair*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    25 Scopus citations

    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.

    Original languageEnglish (US)
    Pages (from-to)4263-4270
    Number of pages8
    JournalBiochemistry
    Volume51
    Issue number21
    DOIs
    StatePublished - May 29 2012

    ASJC Scopus subject areas

    • Biochemistry

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