title: Resolution of DL-hydantoins by D-hydantoinase from Vigna angularis: production of highly enantioenriched N-carbamoyl-D-phenylglycine at 100% conversion.
abstract: 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, Ncarbamoyl-D-phenylglycine was obtained in quantitative yield and over 98% ee.
authors: Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, RJ, Brasil.
authors: M B
authors: MB
authors: Arcuri
authors: O A
authors: OA
authors: Antunes
authors: S J
authors: SJ
authors: Sabino
authors: G F
authors: GF
authors: Pinto
authors: E G
authors: EG
authors: Oestreicher
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D006827:Hydantoins / Q000378:metabolism*; D006868:Hydrolysis; D008968:Molecular Conformation; D010648:Phenylacetates / Q000378:metabolism*; D019685:Rosales / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism*; D013379:Substrate Specificity; D014508:Urea / Q000031:analogs & derivatives* / Q000378:metabolism*
chemical_list: D006827:Hydantoins; D010648:Phenylacetates; C096868:N-carbamyl(phenyl)glycine; D014508:Urea; D000581:Amidohydrolases; C020047:dihydropyrimidinase