Publikation: Studies with Old Yellow Enzyme, Reconstruction with Lumazine Analogs as Coenzyme
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8-Substituted lumazines can be regarded as "mutilated" flavins i.e. isoalloxazines lacking the benzene moiety. The 5'phosphorylated, 8-ribityl derivative binds to the apoenzyme of Old Yellow Enzyme with a Kd which is comparable to that of FMN (Kd 6x10-9 M, and 4x10-10 M for the analog, and FMN respectively). Binding induces profound spectral effects on the lumazine chromophore; this might be interpreted as reflecting a protein induced 7alpha-> 1 prototropy. The complex shows approx. 10% of the catalytic activity of native enzyme, in the oxidation of NADPH. Binding of aromatic molecules known to result in pronounced charge transfer spectra with native old yellow enzyme, have no spectral effect with the analog. These results indicate that the benzene moiety is important for the spectral effect, but not for catalysis.
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WETZEL, Günter, Sandro GHISLA, 1983. Studies with Old Yellow Enzyme, Reconstruction with Lumazine Analogs as Coenzyme. In: BLAIR, John A., ed.. Chemistry and Biology of Pteridines. Berlin: de Gruyter, 1983, pp. 693-698BibTex
@incollection{Wetzel1983Studi-6580, year={1983}, title={Studies with Old Yellow Enzyme, Reconstruction with Lumazine Analogs as Coenzyme}, publisher={de Gruyter}, address={Berlin}, booktitle={Chemistry and Biology of Pteridines}, pages={693--698}, editor={Blair, John A.}, author={Wetzel, Günter and Ghisla, Sandro} }
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