On the catalytic mechanism of prokaryotic leader peptidase 1.

@article{Black1992OnTC,
  title={On the catalytic mechanism of prokaryotic leader peptidase 1.},
  author={M. T. Black and J. G. R. Munn and A E Allsop},
  journal={The Biochemical journal},
  year={1992},
  volume={282 ( Pt 2)},
  pages={539-43}
}
The catalytic mechanism of leader peptidase 1 (LP1) of the bacterium Escherichia coli has been investigated by a combination of site-directed mutagenesis, assays of enzyme activity in vivo utilizing a strain of E. coli which has a conditional defect in LP1 activity, and gene cloning. The biological activity of mutant forms of E. coli LP1 demonstrates that this enzyme belongs to a novel class of proteinases. The possibility that LP1 may be an aspartyl proteinase has been excluded on the basis of… CONTINUE READING

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