Structure-function relationship of bromelain isoinhibitors from pineapple stem.

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 Chem

journal_title

Biological chemistry

authors

Hatano K,Sawano Y,Tanokura M

doi

10.1515/BC.2002.126

keywords:

subject

Has Abstract

pub_date

2002-07-01 00:00:00

pages

1151-6

issue

7-8

eissn

1431-6730

issn

1437-4315

journal_volume

383

pub_type

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