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New Developments in the Synthesis of Natural and Unnatural Amino Acids

1992; Wiley; Volume: 672; Issue: 1 Linguagem: Inglês

10.1111/j.1749-6632.1992.tb35665.x

1749-6632

J. Kamphuis, E. M. Meijer, Wilhelmus H. J. Boesten, Theo Sonke, W. J. J. van den Tweel, H. Schoemaker,

Enzyme Structure and Function

SUMMARY Amino acids play an important role in biochemistry and chemistry. They are the building blocks of proteins and play an essential role in the regulation of the metabolism of living organisms. In general, it can be stated that microbial processes (fermentation) are the industrial production methods of choice for large‐scale production of naturally occuring proteinogenic L‐α‐ H ‐amino acids, while for the production of synthetic D‐ and/or L‐α‐ H ‐amino acids, several other methods are highly competitive. At DSM, several routes, i.e., (chemoenzymatic) synthesis, towards L‐α ‐H and D‐α‐ H ‐amino acids have been elaborated since the midseventies. A general process for the synthesis of natural as well as synthetic optically pure amino acids has been developed, using an enzymatic kinetic resolution step on racemic amino acid amides as the key step. In this case, both enantiomers of the α‐ H ‐amino acids are prepared in one single step. This process has been commercialized since 1988. More recent developments using L‐ or D‐amino peptidases in combination with amino acid amide racemases and an asymmetric transformation concept are discussed.