Applied Microbiology and Biotechnology

, Volume 94, Issue 5, pp 1221–1231 | Cite as

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

Biotechnologically relevant enzymes and proteins

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.

Keywords

Beta-amino acid Hydantoinase Dihydropyrimidinase Carbamoylase 

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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  1. 1.Karlsruhe Institute of Technology (KIT)Institute of Process Engineering in Life Sciences, Section II: Technical BiologyKarlsruheGermany

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