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- W2076179963 abstract "Abstract The Gram-positive bacterium Rhodococcus opacus DSM 43250 produces an l -amino acid oxidase ( l -AAO) with a very broad substrate specificity. This enzyme has been purified to homogeneity and a detailed biochemical characterization was carried out. The complete nucleotide sequence of the l -AAO gene was determined and the primary structure of l -AAO was deduced. The molecular mass of the native enzyme was 99 kDa determined by gel filtration, 54.2/108.5 kDa measured by MALDI-TOF/MS, 53.2 kDa for the subunit calculated after SDS/PAGE. The coenzyme-binding motif G–X–G–X–X–G which is known for all l -AAOs was found very close to the N-terminus of the protein. l -AAO oxidized 39 out of 43 tested l -amino acids. The kinetic data for 16 of these l -amino acids were determined revealing Km-values in the range of 15–30 μM for substrates like l -phenylalanine, l -leucine, l -citrulline and l -lysine. The stability of l -AAO can be increased by storage or incubation of the enzyme in glycine/NaOH buffer. The protein has a pI of 4.8 and a slightly basic pH-optimum at pH 8–9 measured for l -alanine, l -phenylalanine and l -leucine as substrates. The ability for resolution of racemic mixtures was investigated and d -amino acids with an enantiomeric excess of >99% were obtained." @default.
- W2076179963 created "2016-06-24" @default.
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- W2076179963 date "2002-07-01" @default.
- W2076179963 modified "2023-09-23" @default.
- W2076179963 title "A new bacterial l-amino acid oxidase with a broad substrate specificity: purification and characterization" @default.
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- W2076179963 doi "https://doi.org/10.1016/s0141-0229(02)00072-8" @default.
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