Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1.

@article{Wang2009EvidenceFB,
  title={Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1.},
  author={Tao Wang and Luming Yin and Eric M. Cooper and Ming-Yih Lai and Seth W. Dickey and Cecile M. Pickart and David Fushman and K. Douglas Wilkinson and Rachel E. Cohen and Cynthia Wolberger},
  journal={Journal of molecular biology},
  year={2009},
  volume={386 4},
  pages={
          1011-23
        }
}
Otubain 1 belongs to the ovarian tumor (OTU) domain class of cysteine protease deubiquitinating enzymes. We show here that human otubain 1 (hOtu1) is highly linkage-specific, cleaving Lys48 (K48)-linked polyubiquitin but not K63-, K29-, K6-, or K11-linked polyubiquitin, or linear alpha-linked polyubiquitin. Cleavage is not limited to either end of a polyubiquitin chain, and both free and substrate-linked polyubiquitin are disassembled. Intriguingly, cleavage of K48-diubiquitin by hOtu1 can be… CONTINUE READING
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