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Imine Reductases, Reductive Aminases, and Amine Oxidases for the Synthesis of Chiral Amines: Discovery, Characterization, and Synthetic Applications.
- Source :
-
Methods in enzymology [Methods Enzymol] 2018; Vol. 608, pp. 131-149. Date of Electronic Publication: 2018 May 21. - Publication Year :
- 2018
-
Abstract
- Synthesis of the chiral amine moiety is a key challenge for synthetic organic chemistry due to its prevalence in many biologically active molecules. Imine reductase and amine oxidase enzymes have enabled the biocatalytic synthesis of a host of chiral amine compounds. In this chapter, procedures for the synthesis of chiral amines using imine reductases (IREDs), the recently discovered IRED homologues reductive aminases, and amine oxidases (AOs) are described. Amine oxidases have been the subject of mutagenesis approaches for improvement of substrate scope. The high-throughput screening method for determining active variants in amine oxidase libraries is illustrated. Finally, in an approach which takes inspiration from nature, many enzymes can be combined with each other in cascade reactions. The incorporation of imine reductase and monoamine oxidase biocatalysts into several cascade reactions, both in vitro and in vivo (where the approach moves toward synthetic biology), is reported.<br /> (© 2018 Elsevier Inc. All rights reserved.)
- Subjects :
- Amines chemistry
Aminohydrolases genetics
Aspergillus niger enzymology
Aspergillus niger genetics
Aspergillus niger metabolism
Bacteria genetics
Bacteria metabolism
Biocatalysis
Escherichia coli enzymology
Escherichia coli genetics
Escherichia coli metabolism
Fungi genetics
Fungi metabolism
Imines chemistry
Imines metabolism
Monoamine Oxidase genetics
Oxidation-Reduction
Oxidoreductases genetics
Stereoisomerism
Streptomyces enzymology
Streptomyces genetics
Streptomyces metabolism
Synthetic Biology methods
Amines metabolism
Aminohydrolases metabolism
Bacteria enzymology
Fungi enzymology
Monoamine Oxidase metabolism
Oxidoreductases metabolism
Protein Engineering methods
Subjects
Details
- Language :
- English
- ISSN :
- 1557-7988
- Volume :
- 608
- Database :
- MEDLINE
- Journal :
- Methods in enzymology
- Publication Type :
- Academic Journal
- Accession number :
- 30173761
- Full Text :
- https://doi.org/10.1016/bs.mie.2018.04.022