Recent Developments in Enzymatic Asymmetric CC Bond Formation

Some of the recent developments in enzymatic asymmetric CC bond formation are described in this review. The close relationship of biocatalysis and biosynthesis is highlighted with a special emphasis on diversity and biogenesis. One focus of this review is the creation of tetrasubstituted carbon ste...

Full description

Saved in:
Bibliographic Details
Published in:Advanced synthesis & catalysis 2012-11, Vol.354 (17), p.3161-3174
Main Author: Mueller, Michael
Format: Article
Language:English
Subjects:
Aldolase
Asymmetry
biocatalysis
Bioconversions. Hemisynthesis
Biological and medical sciences
biomimetic synthesis
biosynthesis
Biotechnology
Bonding
C1 building blocks
Carbon
Catalysis
Catalysts: preparations and properties
Chemistry
CC coupling
Enzymes
Exact sciences and technology
Free radicals chemistry
Fundamental and applied biological sciences. Psychology
General and physical chemistry
Kinetics and mechanisms
Methods. Procedures. Technologies
Methylation
Organic chemistry
Radicals
Reactivity and mechanisms
Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry
Transformations
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Some of the recent developments in enzymatic asymmetric CC bond formation are described in this review. The close relationship of biocatalysis and biosynthesis is highlighted with a special emphasis on diversity and biogenesis. One focus of this review is the creation of tetrasubstituted carbon stereocenters. Members of the supposedly well‐known aldolase and hydroxynitrile lyase enzyme families possess the ability to catalyze the formation of tertiary alcohols. In the case of aldolases, this can occur through intramolecular cyclization or intermolecular asymmetric CC bond formation. Thiamine diphosphate‐dependent YerE has been identified as a potent catalyst for the acyloin condensation with ketones as acceptor substrates. C1 transformations such as methylation or carboxylation are catalyzed in an asymmetric manner by enzymes from different classes, for example S‐adenosylmethionine‐dependent (radical) enzymes or NADPH‐dependent oxidoreductases. Insights from biosynthetic and mechanistic studies of enzymatic reactions proceeding via radical intermediates give valuable hints towards possible applications in biocatalysis. Still, the oxygen sensitivity of many of these biocatalysts poses a considerable challenge for practical applications.
ISSN:1615-4150
1615-4169
DOI:10.1002/adsc.201100655