title: Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases.
abstract: In this study, we investigated the possibility of using a modified hydantoinase process for the production of optically pure β-amino acids. Two aryl-substituted dihydropyrimidines D,L-6-phenyl-5,6-dihydrouracil (PheDU) and para-chloro-D,L-6-phenyl-5,6-dihydrouracil (pClPheDU) were synthesized. Hydrolysis of these novel substrates to the corresponding N-carbamoyl-β-amino acids by three recombinant D-hydantoinases and several bacterial strains was tested. All applied recombinant D-hydantoinases and eight bacterial isolates catalyzed the conversion of PheDU to N-carbamoyl-β-phenylalanine (NCβPhe). Some of these biocatalysts showed an enantioselectivity for either the D- or the L-PheDU enantiomer. The second dihydropyrimidinase substrate pClPheDU was hydrolyzed by all three recombinant D-hydantoinases and six of the wild-type strains. To our knowledge, this is the first dihydropyrimidinase activity reported with this aryl-substituted dihydropyrimidine. For selected biocatalysts, hydantoinase activity towards aryl-substituted hydantoins was demonstrated as well. However, none of the bacterial strains tested so far exhibited any carbamoylase activity towards NCβPhe.
authors: Karlsruhe Institute of Technology (KIT), Institute of Process Engineering in Life Sciences, Karlsruhe, Germany. ulrike.bretschneider@kit.edu
authors: U
authors: U
authors: Engel
authors: C
authors: C
authors: Syldatk
authors: J
authors: J
authors: Rudat
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D001419:Bacteria / Q000302:isolation & purification / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D011743:Pyrimidines / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D017422:Sequence Analysis, DNA
chemical_list: D011743:Pyrimidines; D011994:Recombinant Proteins; D000581:Amidohydrolases; C020047:dihydropyrimidinase