Conformational Changes in Bovine-Liver Glutamate Dehydrogenase: a Spin-Label Study
نویسندگان
چکیده
منابع مشابه
A product-inhibition study of bovine liver glutamate dehydrogenase.
1. Initial rates of oxidative deamination of L-glutamate with NAD+ as coenzyme, and of reductive aminiation of 2-oxoglutarate with NADH as coenzyme, catalysed by bovine liver glutamate dehydrogenase were measured in 0.111 M-sodium phosphate buffer, pH 7, at 25 degrees C, in the absence and presence of product inhibitors. All 12 possible combinations of variable substrate and product inhibitor w...
متن کاملBinding studies of a spin-labelled oxidized coenzyme to bovine-liver glutamate dehydrogenase.
NAD+ with a nitroxide piperidine ring linked to the NH2 group of the adenine possesses full coenzymatic activity with glutamate dehydrogenase. Electron spin resonance spectra in the presence of glutamate dehydrogenase show mixtures of free and strongly immobilized spin-label. Binding studies in phosphate buffer demonstrate: (a) weak binary binding to the enzyme with a dissociation constant in t...
متن کاملConformational changes and the regulation of glutamate-dehydrogenase activity.
1. The effect of NADH and the non-competitive inhibitor GTP on the optical-rotatory-dispersion properties of glutamate dehydrogenase has been studied. 2. Analysis of the data in terms of the a(0) and b(0) parameters of the Moffitt-Yang equation indicates that a conformational change is induced either by NADH or by GTP in the presence of small amounts of NADH. 3. Sedimentation measurements under...
متن کاملThe Interaction of Tetraiodofluorescein with Glutamate Dehydrogenase from Bovine Liver
Reports from various laboratories have dealt with the binding properties of glutamate dehydrogenase from bovine liver (EC 1.4.1.3) (Pantaloni & Dessen, 1969; Huang & Frieden, 1969; Malcolm, 1972; Brown et al., 1973; Koberstein & Sund, 1973), but unfortunately these reports differ considerably over the number and nature of glutamate dehydrogenase coenzyme-binding sites as well as the magnitude o...
متن کاملMolecular interactions of competitive inhibitors with bovine liver glutamate dehydrogenase.
Four structural analogues of L-glutamate (glutaric acid, thiodiglycolic acid, oxydiglycolic acid, and iminodiacetic acid) were tested for inhibition as a function of pH, of coenzyme NADP+ or NAD+, and of their electronic properties as determined from molecular orbital theory considerations. Plots of pV,., and p(K,/V,,,) versus pH for the uninhibited and inhibited reaction of the oxidative deami...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb13058.x