Interaction of Proteus mirabilis urease apoenzyme and accessory proteins identified with yeast two-hybrid technology.

@article{Heimer2001InteractionOP,
  title={Interaction of Proteus mirabilis urease apoenzyme and accessory proteins identified with yeast two-hybrid technology.},
  author={Susan R. Heimer and Harry L. T. Mobley},
  journal={Journal of bacteriology},
  year={2001},
  volume={183 4},
  pages={1423-33}
}
Proteus mirabilis, a gram-negative bacterium associated with complicated urinary tract infections, produces a metalloenzyme urease which hydrolyzes urea to ammonia and carbon dioxide. The apourease is comprised of three structural subunits, UreA, UreB, and UreC, assembled as a homotrimer of individual UreABC heterotrimers (UreABC)(3). To become catalytically active, apourease acquires divalent nickel ions through a poorly understood process involving four accessory proteins, UreD, UreE, UreF… CONTINUE READING
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