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- W1837931426 abstract "1. The circular dichroism (CD) spectra of the apo- and holoenzyme of D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3] in the far-ultraviolet region were analysed by a curve-fitting technique using the data for poly-L-lysine. The results indicate that the apoenzyme contains 17% β-helix, 32% β-structure, and 51% unordered conformation, and the holoenzyme 16% β-helix, 38% β-structure, and 46% unordered conformation. 2. The CD spectrum of the holoenzyme in the near-ultraviolet region exhibits a negative band around 297 nm, a sharp positive band at 289 nm and a broad positive band ranging from 255 to 275 nm, differing from that of the apoenzyme. The sharp positive band at 289 nm seems to be ascribable to the contribution of tryptophanyl residues, suggesting that conformational change occurs in the apoenzyme upon complex formation with the coenzyme." @default.
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- W1837931426 date "1974-07-01" @default.
- W1837931426 modified "2023-09-25" @default.
- W1837931426 title "Structure and Function of D-Amino Acid Oxidase" @default.
- W1837931426 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a130533" @default.
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