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Processing of the Papain Precursor THE IONIZATION...
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