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Biochemistry. 2012 May 29;51(21):4263-70. doi: 10.1021/bi2016926. Epub 2012 May 17.

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

Author information

1
Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.

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.

PMID:
22564171
PMCID:
PMC4316821
DOI:
10.1021/bi2016926
[Indexed for MEDLINE]
Free PMC Article

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