Related resources
Full-text held externally
Search for item elsewhere
University researcher(s)
Academic department(s)
Enzyme-Catalyzed Enantioselective Hydrolysis of Dihydrouracils as a Route to Enantiomerically Pure beta-Amino Acids
O'Neill, Maeve; Hauer, Bernhard; Schneider, Nina; Turner, Nicholas J
Acs Catalysis. 2011;1(9):1014-1016.
Access to files
Full-text and supplementary files are not available from Manchester eScholar. Full-text is available externally using the following links:
Full-text held externally
Abstract
The hydantoinase from Vigna angularis has been shown to catalysis the hydrolysis of a range of racemic 6-substituted dihydrouracils to yield the corresponding N-carbamoyl-(S)-beta-amino acids and unreacted (R)-dihydrouracils. High enantioselectivity (E > 100) was achieved in cases that the C-6 substituent was an aryl group. Subsequent treatment of the N-carbamoyl derivatives with nitrous acid yielded the free beta-amino acid.
Bibliographic metadata
- Related website <Go to ISI>://WOS:000294704500005
- Times Cited: 0