The folding and activity of the extracellular lipase of Rhizopus oryzae are modulated by a prosequence.

@article{Beer1996TheFA,
  title={The folding and activity of the extracellular lipase of Rhizopus oryzae are modulated by a prosequence.},
  author={H. T. de Beer and Gerd Wohlfahrt and Rolf D. Schmid and John G. McCarthy},
  journal={The Biochemical journal},
  year={1996},
  volume={319 ( Pt 2)},
  pages={351-9}
}
The fungus Rhizopus oryzae synthesizes an extracellular lipase precursor bearing N-terminal pre- and pro-sequences. Our studies in Escherichia coli and using recombinant lipase in vitro indicate that the prosequence of 97 amino acids has at least two functions. First, it modulates the enzyme activity of the lipase so that this enzyme can initially be synthesized in a non-destructive form. Direct synthesis of the mature form of the lipase in the cell has toxic consequences, at least partly… CONTINUE READING

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