Biochemical properties of purified recombinant human beta-carotene 15,15'-monooxygenase.

@article{Lindqvist2002BiochemicalPO,
  title={Biochemical properties of purified recombinant human beta-carotene 15,15'-monooxygenase.},
  author={Annika Lindqvist and Stefan Andersson},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 26},
  pages={23942-8}
}
Beta-carotene 15,15'-monooxygenase (BCO), formerly known as beta-carotene 15,15'-dioxygenase, catalyzes the first step in the synthesis of vitamin A from dietary carotenoids. We have biochemically and enzymologically characterized the purified recombinant human BCO enzyme. A highly active BCO enzyme was expressed and purified to homogeneity from baculovirus-infected Spodoptera frugiperda 9 insect cells. The K(m) and V(max) of the enzyme for beta-carotene were 7 microm and 10 nmol retinal/mg x… CONTINUE READING
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