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K.-i. Hatano, Y. Sawano, M. Tanokura

Structure-Function Relationship of Bromelain Isoinhibitors from Pineapple Stem

Bromelain isoinhibitors from pineapple stem (BIs) are unique doublechain inhibitors and inhibit the cysteine proteinase bromelain competitively. The threedimensional structure was shown to be composed of two distinct domains, each of which is formed by a threestranded antiparallel ?sheet. Unexpectedly, BIs were found to share similar folding and disulfidebond connectivities not with the cystatin superfamily, but with BowmanBirk 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.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 383, 08/2002
Pages: 1151 - 1156

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