Resolution of DL-hydantoins by D-hydantoinase from Vigna angularis: production of highly enantioenriched N-carbamoyl-D-phenylglycine at 100% conversion.
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.
Arcuri
M B
MB
Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, RJ, Brasil.
Antunes
O A
OA
Sabino
S J
SJ
Pinto
G F
GF
Oestreicher
E G
EG
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*
D006827:Hydantoins; D010648:Phenylacetates; C096868:N-carbamyl(phenyl)glycine; D014508:Urea; D000581:Amidohydrolases; C020047:dihydropyrimidinase