CC Hydrolases for Biocatalysis
Autor: | Annika Frank, Wolfgang Kroutil, Gideon Grogan, Elina Siirola |
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Rok vydání: | 2013 |
Předmět: |
chemistry.chemical_classification
0303 health sciences Proteases biology Stereochemistry 030302 biochemistry & molecular biology Enantioselective synthesis General Chemistry biology.organism_classification Cofactor 03 medical and health sciences Kynureninase Enzyme chemistry Biochemistry Biocatalysis Hydrolase biology.protein Rhodococcus 030304 developmental biology |
Zdroj: | Advanced Synthesis & Catalysis. 355:1677-1691 |
ISSN: | 1615-4150 |
DOI: | 10.1002/adsc.201300232 |
Popis: | 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 β-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. |
Databáze: | OpenAIRE |
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