Primary structure of a precursor to the aspartic proteinase from Rhizomucor miehei shows that the enzyme is synthesized as a zymogen.

@article{Boel1986PrimarySO,
  title={Primary structure of a precursor to the aspartic proteinase from Rhizomucor miehei shows that the enzyme is synthesized as a zymogen.},
  author={E Boel and Annelise Bech and K I Randrup and Birgit Dr{\"a}ger and Niels P. Fiil and Bent Foltmann},
  journal={Proteins},
  year={1986},
  volume={1 4},
  pages={363-9}
}
In order to characterize the zymogen of the milk-clotting enzyme from Rhizomucor miehei, we constructed a cDNA library on pBR327 in Escherichia coli. Aspartic proteinase-specific recombinants were isolated by colony hybridization to a specific oligonucleotide mixture, and the cDNA sequence corresponding to a precursor form of the enzyme was determined. The deduced amino acid sequence shows that this secreted fungal proteinase is synthesized as a precursor. The first 22 amino acid residues in… CONTINUE READING