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- W2001672023 abstract "Urea, guanidine hydrochloride, and neutral salts both activate and denature pyridoxamine (pyridoxine) 5′-phosphate oxidase (EC 1.4.3.5) from rabbit liver. Activation occurs at lower concentrations (e.g. 2-2.5 m for urea) of these compounds and is rapid and reversible. Greater structural changes leading to inactivation occur slowly under “activating conditions” but rapidly at higher concentrations of urea. Both reversibly and irreversibly inactivated species are formed. Activation by urea does not involve either dissociation of the enzyme to subunits or aggregation to multimers, and there is little disruption of protein secondary structure. The V and Km for substrates, Ki for product, and the rate of release of product from the enzyme are increased by urea, and substrate inhibition is decreased; urea has little effect on the reactivity of reduced enzyme with oxygen. Both flavin and tryptophanyl fluorescence increase in the presence of urea; at lower concentrations of urea (≤2 m), there is a rapid increase followed by slower, sigmoidal increases. The polarization of flavin fluorescence of the oxidase is increased upon the addition of 2 m urea, which corresponds to the initial enhancement of protein and flavin fluorescence intensities, and then decreases. The near-ultraviolet-visible absorption spectra of native enzyme and that treated with 2 m urea are only slightly different; however, a considerable change at the flavin-binding site is reflected by the circular dichroism spectra. Hence, it appears that urea yields a rapidly formed, “activated” species of the oxidase that is changed primarily at the active site in a manner that allows increased dissociation of substrate and product." @default.
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- W2001672023 date "1966-03-01" @default.
- W2001672023 modified "2023-09-24" @default.
- W2001672023 title "Optical rotatory dispersion of flavin nucleotides" @default.
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- W2001672023 doi "https://doi.org/10.1016/0006-291x(66)90207-5" @default.
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