Catalytic Mechanisms and Biocatalytic Applications of Aspartate and Methylaspartate Ammonia Lyases
| Autor: | Marianne de Villiers, Hans Raj, Vinod Puthan Veetil, Gerrit J. Poelarends, Jandre de Villiers |
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| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular ARGININOSUCCINATE LYASE Ammonia-Lyases MICROCOCCUS DENITRIFICANS Deamination Protein Engineering Aspartate ammonia-lyase Aspartate Ammonia-Lyase Biochemistry BETA-HYDROXYASPARTATE PATHWAY Catalysis Ammonia Catalytic Domain NUCLEOTIDE-SEQUENCE Organic chemistry CRYSTAL-STRUCTURE AMINO-ACIDS L-THREO-3-HYDROXYASPARTATE DEHYDRATASE Bacteria biology Chemistry ACTIVE-SITE Active site BACILLUS SP YM55-1 General Medicine Lyase Enantiopure drug Biocatalysis ESCHERICHIA-COLI biology.protein Molecular Medicine |
| Zdroj: | ACS chemical biology. 7(10):1618-1628 |
| ISSN: | 1554-8929 |
| Popis: | Ammonia lyases catalyze the formation of alpha-beta-unsaturated bonds by the elimination of ammonia from their substrates. This conceptually straightforward reaction has been the emphasis of many studies, with the main focus on the catalytic mechanism of these enzymes and/or the use of these enzymes as catalysts for the synthesis of enantiomerically pure a-amino acids. In this Review aspartate ammonia lyase and 3-methylaspartate ammonia lyase, which represent two different enzyme superfamilies, are discussed in detail. In the past few years, the three-dimensional structures of these lyases in complex with their natural substrates have revealed the details of two elegant catalytic strategies. These strategies exploit similar deamination mechanisms that involve general-base catalyzed formation of an enzyme-stabilized enolate anion (aci-carboxylate) intermediate. Recent progress in the engineering and application of these enzymes to prepare enantiopure L-aspartic acid derivatives, which are highly valuable as tools for biological research and as chiral building blocks for pharmaceuticals and food additives, is also discussed. |
| Databáze: | OpenAIRE |
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