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

Research output: Contribution to journalArticlepeer-review


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
Issue number21
StatePublished - May 29 2012

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration'. Together they form a unique fingerprint.

Cite this