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Human pterin-4 alpha-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor-1 alpha

Human pterin-4 alpha-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor-1 alpha

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KÖSTER, Sandra, Beat THÖNY, Peter MACHEROUX, Hans-Christoph CURTIUS, Claus W. HEIZMANN, Wolfgang PFLEIDERER, Sandro GHISLA, 1995. Human pterin-4 alpha-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor-1 alpha. In: European Journal of Biochemistry. 231(2), pp. 414-423. ISSN 0014-2956. eISSN 1432-1033

@article{Koster1995Human-7375, title={Human pterin-4 alpha-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor-1 alpha}, year={1995}, number={2}, volume={231}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={414--423}, author={Köster, Sandra and Thöny, Beat and Macheroux, Peter and Curtius, Hans-Christoph and Heizmann, Claus W. and Pfleiderer, Wolfgang and Ghisla, Sandro} }

Ghisla, Sandro 2011-03-24T17:33:55Z 1995 Curtius, Hans-Christoph Thöny, Beat Köster, Sandra Heizmann, Claus W. Macheroux, Peter eng Curtius, Hans-Christoph First publ. in: European Journal of Biochemistry 231 (1995), 2, pp. 414-423 Pfleiderer, Wolfgang 2011-03-24T17:33:55Z Pfleiderer, Wolfgang deposit-license Human pterin-4 alpha-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor-1 alpha Köster, Sandra Heizmann, Claus W. Ghisla, Sandro Thöny, Beat Pterin-4a-carbinolamine dehydratase/dimerization cofactor for hepatocyte nuclear factor-1α is a protein with two different functions. We have overexpressed and purified the human wild-type protein, and its Cys81Ser and Cys81Arg mutants. The Cys81Arg mutant has been proposed to be causative in a hyperphenylalaninaemic patient [Citron, B. A., Kaufman, S., Milstien, S., Naylor, E. W., Greene, C. L. & Davis, M. D. (1993) Am. J. Hum. Genet. 53, 768 774]. The dehydratase behaves as a tetramer on gel filtration, while cross-linking experiments showed mono-, di-, tri-, and tetrameric forms, irrespective of the presence of the single Cys81. Sulfhydryl-modifying reagents did not affect the activity, but rather showed that Cys81 is exposed. Various pterins bind and quench the tryptophan fluorescence suggesting the presence of a specific binding site. The fluorescence is destroyed upon light irradiation. Wild-type and the Cys81Ser protein enhance the rate of the phenylalanine hydroxylase assay ≈ 10-fold, a value similar to that of native dehydratase from rat liver; the Cys81Arg mutant, in contrast, has significantly lower activity. This is compatible with the hypothesis that the dehydratase is a rate-limiting factor for the in vivo phenylalanine hydroxylase reaction. The three proteins enhance the spontaneous dehydration of the synthetic substrate 6,6-dimethyl-7,8-dihydropterin-4a-carbinolamine ≈50 70-fold at 4°C and pH 8.5. The results are discussed in view of the recently solved three-dimensional structure of the enzyme [Ficner, R., Sauer, U. W., Stier, G. & Suck, D. (1995) EMBO J. 14, 2032 2042]. Macheroux, Peter application/pdf

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