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Open Access Open Badges Original article

Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences

Ulrike Engel*, Christoph Syldatk and Jens Rudat

Author Affiliations

Karlsruhe Institute of Technology (KIT), Institute of Process Engineering in Life Sciences: Section II: Technical Biology, Engler-Bunte-Ring 1, 76131 Karlsruhe, Germany

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AMB Express 2012, 2:33  doi:10.1186/2191-0855-2-33

Published: 27 June 2012


The amidase activities of two Aminobacter sp. strains (DSM24754 and DSM24755) towards the aryl-substituted substrates phenylhydantoin, indolylmethyl hydantoin, D,L-6-phenyl-5,6-dihydrouracil (PheDU) and para-chloro-D,L-6-phenyl-5,6-dihydrouracil were compared. Both strains showed hydantoinase and dihydropyrimidinase activity by hydrolyzing all substrates to the corresponding N-carbamoyl-α- or N-carbamoyl-β-amino acids. However, carbamoylase activity and thus a further degradation of these products to α- and β-amino acids was not detected. Additionally, the genes coding for a dihydropyrimidinase and a carbamoylase of Aminobacter sp. DSM24754 were elucidated. For Aminobacter sp. DSM24755 a dihydropyrimidinase gene flanked by two genes coding for putative ABC transporter proteins was detected. The deduced amino acid sequences of both dihydropyrimidinases are highly similar to the well-studied dihydropyrimidinase of Sinorhizobium meliloti CECT4114. The latter enzyme is reported to accept substituted hydantoins and dihydropyrimidines as substrates. The deduced amino acid sequence of the carbamoylase gene shows a high similarity to the very thermostable enzyme of Pseudomonas sp. KNK003A.

Beta-amino acid; Dihydropyrimidinase; Hydantoinase; Carbamoylase