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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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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.

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Authors and Affiliations

  1. Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Rio de Janeiro, Brasil, , , , , , BR

    M. B. Arcuri, O. A. C. Antunes, S. J. Sabino, G. F. Pinto & E. G. Oestreicher

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  1. M. B. Arcuri
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  2. O. A. C. Antunes
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  3. S. J. Sabino
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  4. G. F. Pinto
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  5. E. G. Oestreicher
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Received February 17, 2000; Accepted April 4, 2000

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Arcuri, M., Antunes, O., Sabino, S. et al. Resolution of dl-hydantoins by d-hydantoinase from Vigna angularis: Production of highly enantioenriched N-carbamoyl-d-phenylglycine at 100% conversion. Amino Acids 19, 477–482 (2000). https://doi.org/10.1007/s007260070025

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  • DOI: https://doi.org/10.1007/s007260070025

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