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Biol Chem. 2002 Jul-Aug;383(7-8):1151-6.

Structure-function relationship of bromelain isoinhibitors from pineapple stem.

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1
Department of Biological Sciences, Faculty of Engineering, Gunma University, Kiryu, Japan.

Abstract

Bromelain isoinhibitors from pineapple stem (BIs) are unique double-chain inhibitors and inhibit the cysteine proteinase bromelain competitively. The three-dimensional structure was shown to be composed of two distinct domains, each of which is formed by a three-stranded anti-parallel beta-sheet. Unexpectedly, BIs were found to share similar folding and disulfide-bond connectivities not with the cystatin superfamily, but with Bowman-Birk trypsin/chymotrypsin inhibitor (BBI). The structural similarity between them suggests that BIs and BBI have evolved from a common ancestor and differentiated in function during the course of molecular evolution.

PMID:
12437100
DOI:
10.1515/BC.2002.126
[Indexed for MEDLINE]
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