Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives

Francesca Paradisi; Stuart Collins; Anita R Maguire; Paul C Engel

doi:10.1016/j.jbiotec.2006.08.008

Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives

J Biotechnol. 2007 Feb 1;128(2):408-11. doi: 10.1016/j.jbiotec.2006.08.008. Epub 2006 Sep 25.

Authors

Francesca Paradisi¹, Stuart Collins, Anita R Maguire, Paul C Engel

Affiliation

¹ UCD Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland.

PMID: 16996633
DOI: 10.1016/j.jbiotec.2006.08.008

Abstract

Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylalanine and three non-natural amino acids (p-F-phenylalanine, p-MeO-phenylalanine and p-CF(3)-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF(3)-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Oxidoreductases / genetics*
Biotransformation
Kinetics
Mutagenesis, Site-Directed / methods*
Phenylalanine / biosynthesis*
Stereoisomerism

Substances

Phenylalanine
Amino Acid Oxidoreductases
phenylalanine oxidase