Proteasome from Thermoplasma acidophilum: a threonine protease.

@article{Seemller1995ProteasomeFT,
  title={Proteasome from Thermoplasma acidophilum: a threonine protease.},
  author={Erika Seem{\"u}ller and Andrei Lupas and Daniela Stock and Jan-Thomas L{\"o}we and Robert Huber and Wolfgang Baumeister},
  journal={Science},
  year={1995},
  volume={268 5210},
  pages={579-82}
}
The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme. Mutation of the residue to serine led to a fully active enzyme, which was over ten times more sensitive to the serine protease inhibitor 3,4-dichloroisocoumarin. In combination with the crystal structure of… CONTINUE READING

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