Abstract
The hydrolytic cleavage of carbon-carbon bonds by beta-diketone hydrolases (E.C. 3.7.1.X) is a biotransformation reaction that has received limited attention. However, studies of purified enzymes of this class have shown that they are simple hydrolases, with no complex cofactor requirement and as such, they may be a source of economical catalysts with potential application in organic synthesis. In this review, recent developments in the study of beta-diketone hydrolases are surveyed, including our own work, which focuses on the first example of an asymmetric reaction catalysed by one of these enzymes-the cleavage of bicyclic beta-diketones to yield keto acids of high optical purity. (C) 2002 Elsevier Science B.V. All rights reserved.
| Original language | English |
|---|---|
| Pages (from-to) | 73-82 |
| Number of pages | 10 |
| Journal | Journal of Molecular Catalysis B : Enzymatic |
| Volume | 19 |
| Publication status | Published - 2 Dec 2002 |
Keywords
- beta-diketone
- hydrolases
- biotransformation
- RETRO-CLAISEN REACTION
- CROTONASE SUPERFAMILY
- SUBSTRATE-SPECIFICITY
- CRYSTAL-STRUCTURE
- DEGRADING ENZYME
- PSEUDOMONAS SP
- COA HYDRATASE
- MECHANISM
- DESYMMETRIZATION
- METABOLISM