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


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.

SUBMITTER: Zou Y 

PROVIDER: S-EPMC4316821 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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

Zou Yaozhong Y   Zhang Houjin H   Brunzelle Joseph S JS   Johannes Tyler W TW   Woodyer Ryan R   Hung John E JE   Nair Nikhil N   van der Donk Wilfred A WA   Zhao Huimin H   Nair Satish K SK  

Biochemistry 20120517 21


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  ...[more]

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