Mechanism and applications of phosphite dehydrogenase

Heather A. Relyea; Wilfred A. Van Der Donk

doi:10.1016/j.bioorg.2005.01.003

Mechanism and applications of phosphite dehydrogenase

Heather A. Relyea, Wilfred A. Van Der Donk

Research output: Contribution to journal › Review article › peer-review

Abstract

Phosphite dehydrogenase catalyzes the NAD⁺-dependent oxidation of hydrogen phosphonate (common name phosphite) to phosphate in what amounts to a formal phosphoryl transfer reaction from hydride to hydroxide. This review places the enzyme in the context of phosphorus redox metabolism in nature and discusses the results of mechanistic investigations into its reaction mechanism. The potential of the enzyme as a NAD(P)H cofactor regeneration system is discussed as well as efforts to engineer the cofactor specificity of the protein.

Original language	English (US)
Pages (from-to)	171-189
Number of pages	19
Journal	Bioorganic Chemistry
Volume	33
Issue number	3
DOIs	https://doi.org/10.1016/j.bioorg.2005.01.003
State	Published - Jun 2005

Keywords

Cofactor regeneration
Dehydrogenase
Phosphite
Phosphoryl transfer

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Drug Discovery
Organic Chemistry

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10.1016/j.bioorg.2005.01.003

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title = "Mechanism and applications of phosphite dehydrogenase",

abstract = "Phosphite dehydrogenase catalyzes the NAD+-dependent oxidation of hydrogen phosphonate (common name phosphite) to phosphate in what amounts to a formal phosphoryl transfer reaction from hydride to hydroxide. This review places the enzyme in the context of phosphorus redox metabolism in nature and discusses the results of mechanistic investigations into its reaction mechanism. The potential of the enzyme as a NAD(P)H cofactor regeneration system is discussed as well as efforts to engineer the cofactor specificity of the protein.",

keywords = "Cofactor regeneration, Dehydrogenase, Phosphite, Phosphoryl transfer",

author = "Relyea, {Heather A.} and {Van Der Donk}, {Wilfred A.}",

note = "Funding Information: Support for this research was provided by the National Institutes of Health (GM 63003).",

year = "2005",

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doi = "10.1016/j.bioorg.2005.01.003",

language = "English (US)",

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journal = "Bioorganic Chemistry",

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T1 - Mechanism and applications of phosphite dehydrogenase

AU - Relyea, Heather A.

AU - Van Der Donk, Wilfred A.

N1 - Funding Information: Support for this research was provided by the National Institutes of Health (GM 63003).

PY - 2005/6

Y1 - 2005/6

N2 - Phosphite dehydrogenase catalyzes the NAD+-dependent oxidation of hydrogen phosphonate (common name phosphite) to phosphate in what amounts to a formal phosphoryl transfer reaction from hydride to hydroxide. This review places the enzyme in the context of phosphorus redox metabolism in nature and discusses the results of mechanistic investigations into its reaction mechanism. The potential of the enzyme as a NAD(P)H cofactor regeneration system is discussed as well as efforts to engineer the cofactor specificity of the protein.

AB - Phosphite dehydrogenase catalyzes the NAD+-dependent oxidation of hydrogen phosphonate (common name phosphite) to phosphate in what amounts to a formal phosphoryl transfer reaction from hydride to hydroxide. This review places the enzyme in the context of phosphorus redox metabolism in nature and discusses the results of mechanistic investigations into its reaction mechanism. The potential of the enzyme as a NAD(P)H cofactor regeneration system is discussed as well as efforts to engineer the cofactor specificity of the protein.

KW - Cofactor regeneration

KW - Dehydrogenase

KW - Phosphite

KW - Phosphoryl transfer

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DO - 10.1016/j.bioorg.2005.01.003

M3 - Review article

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AN - SCOPUS:15444368832

SN - 0045-2068

VL - 33

SP - 171

EP - 189

JO - Bioorganic Chemistry

JF - Bioorganic Chemistry

IS - 3

ER -

Mechanism and applications of phosphite dehydrogenase

Abstract

Keywords

ASJC Scopus subject areas

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