Literature DB >> 11128554

Resolution of DL-hydantoins by D-hydantoinase from Vigna angularis: production of highly enantioenriched N-carbamoyl-D-phenylglycine at 100% conversion.

M B Arcuri1, O A Antunes, S J Sabino, G F Pinto, E G Oestreicher.   

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.

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Year:  2000        PMID: 11128554     DOI: 10.1007/s007260070025

Source DB:  PubMed          Journal:  Amino Acids        ISSN: 0939-4451            Impact factor:   3.520


  1 in total

1.  Crystallization and preliminary crystallographic studies of the recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114.

Authors:  Sergio Martínez-Rodríguez; Luis Antonio González-Ramírez; Josefa María Clemente-Jiménez; Felipe Rodríguez-Vico; Francisco Javier Las Heras-Vázquez; Jose A Gavira; Juan Manuel García-Ruíz
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-11-30
  1 in total

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