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- W58415003 abstract "Salts of Ma 2+ , Ca 2+ , Y 3+ , Mn 2+ , Fe 3+ , Co 2+ , Ni 2+ , Cu 2+ , Zn 2+ , La 3+ , Ce 3+ , Pr 3+ , Nd 3+ , Sm 3+ , Eu 3+ , Gd 3+ , Tb 3+ , Dy 3+ , Ho 3+ , Er 3+ , Tm 3+ , Yb 3+ and Lu 3+ were investigated as effectors of the horse liver aldehyde dehydrogenase isoenzymes, F1 and F2. While Ca 2+ and Mg 2+ were relatively insensitive effectors (requiring > 200 μM concentrations), most remaining metal ions produced dramatic activation (0.1–10μM) and inhibition (5–40 μM) with the F1 isoenzyme and large activation but weak inhibition with the F2 isoenzyme. The representative pattern of activation and inhibition of F1 with Zn 2+ possessed a maximal 200% activation (0.5μM) followed by 90% inhibition (2.0 μM Zn 2+ ) with 1 mM acetaldehyde and 0.1 mM NAD + . The stoichiometry of NADH binding established by fluorescence titration with Fl in the presence of inhibitory levels of Zn 2+ was shown to be two moles of NADH per mole of enzyme. Tigher NADH binding to the enzyme was noted. The tighter binding of NADH could be the mechanism of Inhibition where the dehydrogenase activity is moderated by the rate limiting NADH dissociation step. Because NAD + is not required, the effect of metal ions upon the esterase activity discriminates as to whether the metal ions are probing the substrate or coenzyme binding sites. Zinc was the only metal ion tested which showed equivalent esterase and dehydrogenase inhibition. This indicates that the dehydrogenase activity is controlled through the binding of metal ions to the cofactor, NAD + , and their corresponding influence upon slower release of NADH." @default.
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- W58415003 date "1977-01-01" @default.
- W58415003 modified "2023-10-16" @default.
- W58415003 title "METAL ION EFFECTORS OF HORSE LIVER ALDEHYDE DEHYDROGENASES" @default.
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- W58415003 doi "https://doi.org/10.1016/b978-0-12-691402-3.50021-4" @default.
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