4.7 Review

C-C Hydrolases for Biocatalysis

Journal

ADVANCED SYNTHESIS & CATALYSIS
Volume 355, Issue 9, Pages 1677-1691

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.201300232

Keywords

asymmetric catalysis; biotransformations; CC hydrolysis; hydrolases

Funding

  1. Marie Curie Network for Initial Training fellowship in the project BIOTRAINS [FP7-PEOPLE-ITN-2008-238531]

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Although CC bond hydrolases are distributed widely in Nature, they has as yet have received only limited attention in the area of biocatalysis compared to their counterpart the C-heteroatom hydrolases, such as lipases and proteases. However, the substrate range of CC hydrolases, and their non-dependence on cofactors, suggest that these enzymes may have considerable potential for applications in synthesis. In addition, hydrolases such as the -diketone hydrolase from Rhodococcus (OCH) are known, that catalyse the formation of interesting chiral intermediates. Further enzymes, such as kynureninase and a meta-cleavage product hydrolase (MhpC), are able to catalyse carbon-carbon bond formation, suggesting wider applications in biocatalysis than previously envisaged. In this review, the distribution, catalytic characteristics and applications of CC hydrolases are described, with a view to assessing their potentialfor use in biocatalytic processes in the future.

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