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

Authors
Arcuri, MB Antunes, OAC Sabino, SJ Pinto, GF Oestreicher, EG
Citation
Mb. Arcuri 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(2), 2000, pp. 477-482
Citations number
10
Categorie Soggetti
Biochemistry & Biophysics
Journal title
AMINO ACIDS
ISSN journal
09394451 → ACNP
Volume
19
Issue
2
Year of publication
2000
Pages
477 - 482
Database
ISI
SICI code
0939-4451(2000)19:2<477:RODBDF>2.0.ZU;2-L
Abstract
D-Hydantoinase from Vigna angularis hydrolyzed rac-5-monosubstituted-hydant oins with polar and aromatic side chains and dihydrothymine but rac-5,5-dis ubstituted-hydantoins were not substrates of this enzyme. 5-Phenylhydantoin was the best substrate. By using this substrate, N-carbamoyl-D-phenylglyci ne was obtained in quantitative yield and over 98% ee.