Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration.

doi:10.1111/j.1742-4658.2005.04788.x

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Article

Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration.

The FEBS journal - 1 Aug 2005

Woodyer Ryan, Zhao Huimin, van der Donk Wilfred A

Abstract excerpt

NAD(P)H regeneration is important for biocatalytic reactions that require these costly cofactors. A mutant phosphite dehydrogenase (PTDH-E175A/A176R) that utilizes both NAD and NADP efficiently is a very promising system for NAD(P)H regeneration. In this work, both the kinetic mechanism and practical application of PTDH-E175A/A176R were investigated for better understanding of the enzyme and to provide a basis...

Topics

Deuterium
Escherichia coli Proteins
Kinetics
Mutation
NAD
NADH, NADPH Oxidoreductases
NADP
Protein Structure, Tertiary
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Structural Homology, Protein
Time Factors
Tryptophan
Xylitol

Source

Open in PubMed

Identifiers

PMID: 16045753
DOI: 10.1111/j.1742-4658.2005.04788.x

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