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

M B Arcuri; O A Antunes; S J Sabino; G F Pinto; E G Oestreicher

doi:10.1007/s007260070025

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

Amino Acids. 2000;19(2):477-82. doi: 10.1007/s007260070025.

Authors

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

Affiliation

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

PMID: 11128554
DOI: 10.1007/s007260070025

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amidohydrolases / metabolism*
Hydantoins / metabolism*
Hydrolysis
Molecular Conformation
Phenylacetates / metabolism*
Rosales / chemistry
Rosales / enzymology
Rosales / metabolism*
Substrate Specificity
Urea / analogs & derivatives*
Urea / metabolism*

Substances

Hydantoins
Phenylacetates
N-carbamyl(phenyl)glycine
Urea
Amidohydrolases
dihydropyrimidinase