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Protein Engineering vol. 8 no. 1 pp. 59-62, 1995
© 1995 Oxford University Press

RESEARCH-ARTICLE

Recombinant pro-regions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes

Mark A.J. Taylor1,2, Kenneth C. Baker1, Geoffrey S. Briggs3,4, Ian F. Connerton1, Nicola J. Cummings1, Kathryn A. Pratt1, Dean F. Revell1, Robert B. Freedman3 and Peter W. Goodenough1

1Protein Engineering Department, Institute of Food Research Earley Gate, Whiteknights Road, Reading RG6 2EF 3Biological Laboratory, University of Kent Canterbury, Kent CT2 7NJ, UK

2To whom correspondence should be addressed

Proteolytic enzymes require the presence of their proregions for correct folding. Of the four proteolytic enzymes from Carica papaya, papain and papaya proteinase IV (PPIV) have 68% sequence identity. We find that their proregions are even more similar, exhibiting 73.6% identity. cDNAs encoding the pro-regions of these two proteinases have been expressed in Escherichia coli independently from their mature enzymes. The recombinant pro-regions of papain and PPIV have been shown to be high affinity inhibitors of all four of the mature native papaya cysteine proteinases. Their inhibition constants are in the range 10–6–;10–;9 M. PPIV was inhibited two to three orders of magnitude less effectively than papain, chymopapain and caricain. The pro-region of PPIV, however, inhibited its own mature enzyme more effectively than did the proregion of papain. Alignment of the sequences of the four papaya enzymes shows that there is a highly variable section towards the C-terminal of the pro-region. This region may therefore confer selectivity to the pro-regions for the individual proteolytic enzymes.

Keywords: cysteine proteinase/inhibition/papain/PPIV/proregion

Received July 15, 1994; revised September 15, 1994; accepted October 19, 1994.


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