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  • Title: alpha-Ketoglutaric acid: solution structure and the active form for reductive amination by bovine liver glutamate dehydrogenase.
    Author: Viswanathan TS, Johnson RE, Fisher HF.
    Journal: Biochemistry; 1982 Jan 19; 21(2):339-45. PubMed ID: 7074017.
    Abstract:
    A study of the various solution forms of alpha-ketoglutaric acid using UV absorption spectrophotometry and 13C NMR spectroscopy shows that at neutral pH alpha-ketoglutarate exists predominantly as the keto form with about 7% hydrated form (gem-diol) and a small amount of cyclic form. Protonation of the gamma-carboxylate group increases the amount of cyclic form to 20% with very little increase in the amount of gem-diol. Protonation of the alpha-carboxylate increases the amount of cyclic form to 30% and the amount of gem-diol to 35%. The pH and temperature dependence of the 13C NMR line widths indicated that the interconversion of keto and cyclic forms is extremely rapid. The rate of interconversion of keto and gem-diol forms was studied spectrophotometrically at various temperatures, buffers, and pH values and by varying the total concentration of alpha-ketoglutarate. The hydration reaction of alpha-ketoglutarate is not catalyzed by bovine liver glutamate dehydrogenase (E) or by the E-NADPH complex. The enzyme uses the keto form of alpha-ketoglutarate as the substrate. The gem-diol form is not itself a substrate but becomes converted to the keto form with a half-life of about 0.3 min at 15 degrees C in 0.1 M potassium phosphate buffer (pH 7.6).
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