Metal ion dependence of recombinant Escherichia coli allantoinase.

@article{Mulrooney2003MetalID,
  title={Metal ion dependence of recombinant Escherichia coli allantoinase.},
  author={Scott B. Mulrooney and Robert P. Hausinger},
  journal={Journal of bacteriology},
  year={2003},
  volume={185 1},
  pages={126-34}
}
Allantoinase is a suspected dinuclear metalloenzyme that catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid. Recombinant Escherichia coli allantoinase purified from overproducing cultures amended with 2.5 mM zinc, 1 mM cobalt, or 1 mM nickel ions was found to possess approximately 1.4 Zn, 0.0 Co, 0.0 Ni, and 0.4 Fe; 0.1 Zn, 1.0 Co, 0.0 Ni, and 0.2 Fe; and 0.0 Zn, 0.0 Co, 0.6 Ni, and 0.1 Fe per subunit, respectively, whereas protein… CONTINUE READING
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