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- W2057331409 abstract "A screening of soil samples for d-amino acid oxidase (d-AAO) activity led to the isolation and identification of the gram-positive bacterium Arthrobacter protophormiae. After purification of the wild-type d-AAO, the gene sequence was determined and designated dao. An alignment of the deduced primary structure with eukaryotic d-AAOs and d-aspartate oxidases showed that the d-AAO from A. protophormiae contains five of six conserved regions; the C-terminal type 1 peroxisomal targeting signal that is typical for d-AAOs from eukaryotic origin is missing. The dao gene was cloned and expressed in Escherichia coli. The purified recombinant d-AAO had a specific activity of 180 U mg protein−1 for d-methionine and was slightly inhibited in the presence of l-methionine. Mainly, basic and hydrophobic d-amino acids were oxidized by the strictly enantioselective enzyme. After a high cell density fermentation, 2.29 × 106 U of d-AAO were obtained from 15 l of fermentation broth." @default.
- W2057331409 created "2016-06-24" @default.
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- W2057331409 date "2007-04-01" @default.
- W2057331409 modified "2023-10-16" @default.
- W2057331409 title "Overproduction and characterization of a recombinant D-amino acid oxidase from Arthrobacter protophormiae" @default.
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- W2057331409 doi "https://doi.org/10.1007/s00253-006-0776-9" @default.
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