Resolution of dl-hydantoins by d-hydantoinase from Vigna angularis: Production of highly enantioenriched N-carbamoyl-d-phenylglycine at 100% conversion |
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| Authors: | M B Arcuri O A C Antunes S J Sabino G F Pinto E G Oestreicher |
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| Institution: | (1) Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Rio de Janeiro, Brasil, BR |
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| Abstract: | Summary.
d-Hydantoinase from Vigna angularis hydrolyzed rac-5-monosubstituted-hydantoins with polar and aromatic side chains and dihydrothymine but rac-5,5-disubstituted-hydantoins were not substrates of this enzyme. 5-Phenylhydantoin was the best substrate. By using this
substrate, N-carbamoyl-d-phenylglycine was obtained in quantitative yield and over 98% ee.
Received February 17, 2000; Accepted April 4, 2000 |
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| Keywords: | : Amino acids – d-Hydantoinase – N-Carbamoyl-d-phenylglycine – Substrate specificity – Vigna angularis |
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