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Verlagsausgabe
DOI: 10.5445/IR/1000033254
Veröffentlicht am 07.05.2018
Originalveröffentlichung
DOI: 10.1186/2191-0855-2-33
Scopus
Zitationen: 2
Web of Science
Zitationen: 2

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

Engel, U.; Syldatk, C.; Rudat, J.

Abstract:
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 ve ... mehr


Zugehörige Institution(en) am KIT Institut für Bio- und Lebensmitteltechnik (BLT)
Publikationstyp Zeitschriftenaufsatz
Jahr 2012
Sprache Englisch
Identifikator ISSN: 2191-0855
URN: urn:nbn:de:swb:90-332549
KITopen ID: 1000033254
Erschienen in AMB express
Band 2
Heft 1
Seiten 33
Schlagworte Beta-amino acid, Dihydropyrimidinase, Hydantoinase, Carbamoylase
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