Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui.

@article{Johnsen2004NovelXD,
  title={Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui.},
  author={Ulrike Johnsen and Peter Sch{\"o}nheit},
  journal={Journal of bacteriology},
  year={2004},
  volume={186 18},
  pages={
          6198-207
        }
}
During growth of the halophilic archaeon Haloarcula marismortui on D-xylose, a specific D-xylose dehydrogenase was induced. The enzyme was purified to homogeneity. It constitutes a homotetramer of about 175 kDa and catalyzed the oxidation of xylose with both NADP+ and NAD+ as cosubstrates with 10-fold higher affinity for NADP+. In addition to D-xylose, D-ribose was oxidized at similar kinetic constants, whereas D-glucose was used with about 70-fold lower catalytic efficiency (kcat/Km). With the… CONTINUE READING
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