Chiral amines are a class of privileged compounds that find application in synthesis of API, fine chemicals, chiral auxiliaries, etc. As such, asymmetric synthesis of important chiral amines through biocatalytic means offers a unique opportunity to encompass exquisite selectivity and clean reaction conditions and more importantly, avoiding the use of transition metals that at the end of the process are difficult to detach from the final product, precluding its ready use. Therefore, a series of enzymes, apart from traditionally used lipases, have been incorporated in the chemist’s toolbox to provide novel solutions in academia and industry.
Among these enzymes, one can find transaminases, imine reductases and amine dehydrogenases as the most prominent ones. Lately, some of these enzymes have been extensively employed in multicatalytic cascade reactions to afford green and sustainable synthetic routes, and their application in flow chemistry together with modern protein engineering of both specificity and stability have further added to their potential as industrial catalysts.
Despite the fact of being very valuable catalysts for the preparation of chiral amines, the application of transaminases, imine reductases and amine dehydrogenases in biocatalytic procedures is still hampered by some drawbacks, including unfavourable chemical equilibrium, low stability, inhibition processes, requirement of cofactors and limited substrate specificity. The development of novel amino donors as well as improved methodologies for efficient equilibrium displacement are also areas of interest when carrying out the synthesis of chiral amines employing these biocatalysts. In order to overcome these issues, in the last few years several efforts have been made to further develop formal enzymatic reductive amination for the preparation of chiral amine-containing compounds in effective processes.
The present collection will be focused in research manuscripts as well as in reviews that cover the following aspects concerning the application of different types of biocatalysts (transaminases, imine reductases, amine dehydrogenases,…) in the preparation of optically active amines.
• Synthesis of valuable compounds employing transaminases, amine dehydrogenases, imine reductases and other biocatalysts.
• Multicatalytic cascade processes involving formal enzymatic reductive amination.
• Immobilization of these enzymes and flow chemistry processes.
• Enzyme engineering for novel substrate specificity and improved stability.
• Metagenomic discovery of new enzymes and genomic origin and relations.
Chiral amines are a class of privileged compounds that find application in synthesis of API, fine chemicals, chiral auxiliaries, etc. As such, asymmetric synthesis of important chiral amines through biocatalytic means offers a unique opportunity to encompass exquisite selectivity and clean reaction conditions and more importantly, avoiding the use of transition metals that at the end of the process are difficult to detach from the final product, precluding its ready use. Therefore, a series of enzymes, apart from traditionally used lipases, have been incorporated in the chemist’s toolbox to provide novel solutions in academia and industry.
Among these enzymes, one can find transaminases, imine reductases and amine dehydrogenases as the most prominent ones. Lately, some of these enzymes have been extensively employed in multicatalytic cascade reactions to afford green and sustainable synthetic routes, and their application in flow chemistry together with modern protein engineering of both specificity and stability have further added to their potential as industrial catalysts.
Despite the fact of being very valuable catalysts for the preparation of chiral amines, the application of transaminases, imine reductases and amine dehydrogenases in biocatalytic procedures is still hampered by some drawbacks, including unfavourable chemical equilibrium, low stability, inhibition processes, requirement of cofactors and limited substrate specificity. The development of novel amino donors as well as improved methodologies for efficient equilibrium displacement are also areas of interest when carrying out the synthesis of chiral amines employing these biocatalysts. In order to overcome these issues, in the last few years several efforts have been made to further develop formal enzymatic reductive amination for the preparation of chiral amine-containing compounds in effective processes.
The present collection will be focused in research manuscripts as well as in reviews that cover the following aspects concerning the application of different types of biocatalysts (transaminases, imine reductases, amine dehydrogenases,…) in the preparation of optically active amines.
• Synthesis of valuable compounds employing transaminases, amine dehydrogenases, imine reductases and other biocatalysts.
• Multicatalytic cascade processes involving formal enzymatic reductive amination.
• Immobilization of these enzymes and flow chemistry processes.
• Enzyme engineering for novel substrate specificity and improved stability.
• Metagenomic discovery of new enzymes and genomic origin and relations.
