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Structure-function Relationship of Bromelain Isoinhibitors From Pineapple Stem

Structure-function Relationship of Bromelain Isoinhibitors From Pineapple Stem

Ken-ichi Hatano, Yoriko Sawano, Masaru Tanokura

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

PMID: 12437100

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP37189347	Bromelain from pineapple stem		37189-34-7	Price

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