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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year

IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
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Volume 383, Issue 7-8


Structure-Function Relationship of Bromelain Isoinhibitors from Pineapple Stem

K.-i. Hatano / Y. Sawano / M. Tanokura
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.126


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 βsheet. 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.

About the article

Published Online: 2005-06-01

Published in Print: 2002-08-27

Citation Information: Biological Chemistry, Volume 383, Issue 7-8, Pages 1151–1156, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.126.

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