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.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Hatano K,Sawano Y,Tanokura Mdoi
10.1515/BC.2002.126keywords:
subject
Has Abstractpub_date
2002-07-01 00:00:00pages
1151-6issue
7-8eissn
1431-6730issn
1437-4315journal_volume
383pub_type
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