Pyruvate:NADP+ oxidoreductase is stabilized by its cofactor, thiamin pyrophosphate, in mitochondria of Euglena gracilis.

@article{Nakazawa2003PyruvateNADPOI,
  title={Pyruvate:NADP+ oxidoreductase is stabilized by its cofactor, thiamin pyrophosphate, in mitochondria of Euglena gracilis.},
  author={Masami Nakazawa and Shigeo Takenaka and Mitsuhiro Ueda and Hiroshi Inui and Yoshihisa Nakano and Kazutaka Miyatake},
  journal={Archives of biochemistry and biophysics},
  year={2003},
  volume={411 2},
  pages={
          183-8
        }
}
Pyruvate:NADP(+) oxidoreductase (PNO) is a thiamin pyrophosphate (TPP)-dependent enzyme that plays a central role in the respiratory metabolism of Euglena gracilis, which requires thiamin for growth. When thiamin was depleted in Euglena cells, PNO protein level was greatly reduced, but its mRNA level was barely changed. In addition, a large part of PNO occurred as an apoenzyme lacking TPP in the deficient cells. The PNO protein level increased rapidly, without changes in the mRNA level, after… CONTINUE READING

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