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

Francesca Paradisi
, Stuart Collins
, Anita R. Maguire
, Paul C. Engel

University College Dublin

Research output: Contribution to journal › Article › peer-review

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-CF₃-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF₃-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.

Original language	English
Pages (from-to)	408-411
Number of pages	4
Journal	Journal of Biotechnology
Volume	128
Issue number	2
DOIs	https://doi.org/10.1016/j.jbiotec.2006.08.008
Publication status	Published - 1 Feb 2007

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 12 Responsible Consumption and Production

Keywords

Biocatalysis
Chiral synthesis
Cofactor recycling
Non-natural amino acids
Phenylalanine dehydrogenase
Site-directed mutagenesis

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10.1016/j.jbiotec.2006.08.008

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title = "Phenylalanine dehydrogenase mutants: Efficient biocatalysts for synthesis of non-natural phenylalanine derivatives",

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-CF3-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF3-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.",

keywords = "Biocatalysis, Chiral synthesis, Cofactor recycling, Non-natural amino acids, Phenylalanine dehydrogenase, Site-directed mutagenesis",

author = "Francesca Paradisi and Stuart Collins and Maguire, \{Anita R.\} and Engel, \{Paul C.\}",

year = "2007",

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T1 - Phenylalanine dehydrogenase mutants

T2 - Efficient biocatalysts for synthesis of non-natural phenylalanine derivatives

AU - Paradisi, Francesca

AU - Collins, Stuart

AU - Maguire, Anita R.

AU - Engel, Paul C.

PY - 2007/2/1

Y1 - 2007/2/1

N2 - 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-CF3-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF3-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.

AB - 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-CF3-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF3-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.

KW - Biocatalysis

KW - Chiral synthesis

KW - Cofactor recycling

KW - Non-natural amino acids

KW - Phenylalanine dehydrogenase

KW - Site-directed mutagenesis

UR - https://www.scopus.com/pages/publications/33846105845

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DO - 10.1016/j.jbiotec.2006.08.008

M3 - Article

C2 - 16996633

AN - SCOPUS:33846105845

SN - 0168-1656

VL - 128

SP - 408

EP - 411

JO - Journal of Biotechnology

JF - Journal of Biotechnology

IS - 2

ER -

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

Abstract

UN SDGs

Keywords

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