Journal article
Processing of the Papain Precursor THE IONIZATION STATE OF A CONSERVED AMINO ACID MOTIF WITHIN THE Pro REGION PARTICIPATES IN THE REGULATION OF INTRAMOLECULAR PROCESSING *
Abstract
The cysteine protease papain is synthesized as a 40-kDa inactive precursor with a 107-amino-acid N-terminal pro region. Although sequence conservation in the pro region is lower than in the mature proteases, a conserved motif (Gly-Xaa-Asn-Xaa-Phe-Xaa-Asp-36, papain precursor numbering) was found within the pro region of cysteine proteases of the papain superfamily. To determinate the function to this conserved motif, we have mutagenized at …
Authors
Vernet T; Berti PJ; de Montigny C; Musil R; Tessier DC; Ménard R; Magny M-C; Storer AC; Thomas DY
Journal
Journal of Biological Chemistry, Vol. 270, No. 18, pp. 10838–10846
Publisher
Elsevier
Publication Date
5 1995
DOI
10.1074/jbc.270.18.10838
ISSN
0021-9258