Literature DB >> 16996633

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

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

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.

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Year:  2006        PMID： 16996633     DOI： 10.1016/j.jbiotec.2006.08.008

Source DB:  PubMed          Journal:  J Biotechnol        ISSN： 0168-1656            Impact factor:   3.307


  5 in total

1.  Crystal structure of a chimaeric bacterial glutamate dehydrogenase.

Authors:  Tânia Oliveira; Michael A Sharkey; Paul C Engel; Amir R Khan
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2016-05-23       Impact factor: 1.056

2.  Overexpression in a non-native halophilic host and biotechnological potential of NAD+-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014.

Authors:  Nayla Munawar; Paul C Engel
Journal:  Extremophiles       Date:  2012-04-19       Impact factor: 2.395

3.  Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases.

Authors:  Michael A Sharkey; Tânia F Oliveira; Paul C Engel; Amir R Khan
Journal:  FEBS J       Date:  2013-08-20       Impact factor: 5.542

4.  Construction and evaluation of a novel bifunctional phenylalanine-formate dehydrogenase fusion protein for bienzyme system with cofactor regeneration.

Authors:  Wei Jiang; Bai-Shan Fang
Journal:  J Ind Microbiol Biotechnol       Date:  2016-01-27       Impact factor: 3.346

5.  Rationally re-designed mutation of NAD-independent L-lactate dehydrogenase: high optical resolution of racemic mandelic acid by the engineered Escherichia coli.

Authors:  Tianyi Jiang; Chao Gao; Peipei Dou; Cuiqing Ma; Jian Kong; Ping Xu
Journal:  Microb Cell Fact       Date:  2012-11-23       Impact factor: 5.328
  5 in total

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