Unknown

Dataset Information

0

On the current role of hydratases in biocatalysis.


ABSTRACT: Water addition to carbon-carbon double bonds provides access to value-added products from inexpensive organic feedstock. This interesting but relatively little-studied reaction is catalysed by hydratases in a highly regio- and enantiospecific fashion with excellent atom economy. Considering that asymmetric hydration of (non-activated) carbon-carbon double bonds is virtually impossible with current organic chemistry, enzymatic hydration reactions are highly attractive for industrial applications. Hydratases have been known for several decades but their biocatalytic potential has only been explored over the past 15 years. As a result, a considerable amount of information on this enzyme group has become available, enabling their development for practical applications. This review focuses on hydratases catalysing water addition to non-activated carbon-carbon double bonds, and examines hydratases from a biochemical, structural and mechanistic angle. Current challenges and opportunities in hydration biocatalysis are discussed, and, ultimately, their potential for organic synthesis is highlighted.

SUBMITTER: Engleder M 

PROVIDER: S-EPMC6013536 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

On the current role of hydratases in biocatalysis.

Engleder Matthias M   Pichler Harald H  

Applied microbiology and biotechnology 20180521 14


Water addition to carbon-carbon double bonds provides access to value-added products from inexpensive organic feedstock. This interesting but relatively little-studied reaction is catalysed by hydratases in a highly regio- and enantiospecific fashion with excellent atom economy. Considering that asymmetric hydration of (non-activated) carbon-carbon double bonds is virtually impossible with current organic chemistry, enzymatic hydration reactions are highly attractive for industrial applications.  ...[more]

Similar Datasets

| S-EPMC4285126 | biostudies-literature
| S-EPMC9038100 | biostudies-literature
| S-EPMC8403116 | biostudies-literature
| S-EPMC8540959 | biostudies-literature
| S-EPMC6441135 | biostudies-literature
2013-09-25 | GSE51145 | GEO
| S-EPMC5324637 | biostudies-literature
| S-EPMC9528183 | biostudies-literature
| S-EPMC7844857 | biostudies-literature
| S-EPMC9491828 | biostudies-literature