Abstract
The acylase from Aspergillus melleus was able to hydrolyse the amide bond of (S)-phenylalanine-N-2-(R,S)-fluoropropionamide and discriminate the diastereoisomers such that the (S,S)-diastereoisomer was hydrolysed by an order of magnitude faster than the (S,R)diasteroisomer. The origin of the kinetic discrimination is attributed to both binding and kinetic effects. (C) 2000 Elsevier Science S.A. All rights reserved.
Original language | English |
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Pages (from-to) | 235-238 |
Number of pages | 4 |
Journal | Journal of Fluorine Chemistry |
Volume | 102 |
Publication status | Published - Mar 2000 |
Keywords
- F-19-NMR
- acylase
- Aspergillus melleus
- alpha-fluoroamide
- enzyme resolution
- PYRIDINE
- FLUORINE