Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast.

@article{Ju2004Human1S,
  title={Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast.},
  author={Shulin Ju and Galit Shaltiel and Alon Shamir and Galila Agam and Miriam L Greenberg},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 21},
  pages={21759-65}
}
We have cloned, sequenced, and expressed a human cDNA encoding 1-d-myo-inositol-3-phosphate (MIP) synthase (hINO1). The encoded 62-kDa human enzyme converted d-glucose 6-phosphate to 1-d-myo-inositol 3-phosphate, the rate-limiting step for de novo inositol biosynthesis. Activity of the recombinant human MIP synthase purified from Escherichia coli was optimal at pH 8.0 at 37 degrees C and exhibited K(m) values of 0.57 mm and 8 microm for glucose 6-phosphate and NAD(+), respectively. NH(4)(+) and… CONTINUE READING

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