Enhancement of the Activity of -Aspartase from Escherichia coli W by Directed Evolution

Wang, Lijuan; Kong, Xiangduo; Zhang, Hongying; Wang, Xiaoping; Jin, Zhang

doi:10.1006/bbrc.2000.3472

Cited by 33 publications

(12 citation statements)

References 10 publications

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“…Therefore, the synthetic use of aspartase is limited to commercial production of its natural substrate from fumaric acid and ammonia with aspartase-containing immobilized cells of Escherichia coli in continuous, fixed-bed operation (5,6). Recombinant production of aspartase enabled the modification of the catalytic properties of the biocatalyst by directed evolution (7,8).…”

Section: Introductionmentioning

confidence: 99%

Preparation of Unnatural Amino Acids with Ammonia-Lyases and 2,3-Aminomutases

Poppe

Paizs

Kovács

et al. 2011

Methods in Molecular Biology

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Ammonia-lyases catalyze a wide range of processes leading to α,β-unsaturated compounds by elimination of ammonia. In this chapter, ammonia-lyases are reviewed with major emphasis on their synthetic applications in stereoselective preparation of unnatural amino acids. Besides the synthesis of various unnatural α-amino acids with the aid of phenylalanine ammonia-lyases (PALs) utilizing the 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) prosthetic groups, the biotransformations leading to various unnatural β-amino acids with phenylalanine 2,3-aminomutases using the same catalytic MIO prosthetic group are discussed. Cloning, production, purification, and biotransformation protocols for PAL are described in detail.

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Section: Introductionmentioning

confidence: 99%

Preparation of Unnatural Amino Acids with Ammonia-Lyases and 2,3-Aminomutases

Poppe

Paizs

Kovács

et al. 2011

Methods in Molecular Biology

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“…More active aspartase biocatalysts have been obtained by cloning and overexpression of the aspartase-encoding gene from Brevibacterium flavum MJ-233 [119] and E. coli [120,121], and by protein engineering via site-directed mutagenesis and directed evolution [122,123]. A highly thermostable aspartase has been identified in Bacillus sp.…”

Section: Ammonia Lyase Processesmentioning

confidence: 99%

Use of Enzymes in the Synthesis of Amino Acids

Sonke

Kaptein

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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“…Seven base changes resulted in three amino acid changes, namely N217K, T233R and V367G, which caused the enhancement of properties. 134 Xylanase is yet another enzyme that falls under the category of enzymes-lyase. Recently, a combination of directed evolution techniques, i.e.…”

Section: Lyasesmentioning

confidence: 99%

Directed Evolution: An Approach to Engineer Enzymes

Kaur

Sharma

2006

Critical Reviews in Biotechnology

126

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Directed evolution is being used increasingly in industrial and academic laboratories to modify and improve commercially important enzymes. Laboratory evolution is thought to make its biggest contribution in explorations of non-natural functions, by allowing us to distinguish the properties nurtured by evolution. In this review we report the significant advances achieved with respect to the methods of biocatalyst improvement and some critical properties and applications of the modified enzymes. The application of directed evolution has been elaborately demonstrated for protein solubility, stability and catalytic efficiency. Modification of certain enzymes for their application in enantioselective catalysis has also been elucidated. By providing a simple and reliable route to enzyme improvement, directed evolution has emerged as a key technology for enzyme engineering and biocatalysis.

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Enhancement of the Activity of -Aspartase from Escherichia coli W by Directed Evolution

Cited by 33 publications

References 10 publications

Preparation of Unnatural Amino Acids with Ammonia-Lyases and 2,3-Aminomutases

Preparation of Unnatural Amino Acids with Ammonia-Lyases and 2,3-Aminomutases

Use of Enzymes in the Synthesis of Amino Acids

Directed Evolution: An Approach to Engineer Enzymes

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