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• W2040236473 abstract "Bromelain inhibitor VI from pineapple stem (BI-VI) is a unique double-chain inhibitor with an 11-residue light chain and a 41-residue heavy chain by disulfide bonds and inhibits the cysteine proteinase bromelain competitively. The structure of BI-VI in aqueous solution was determined using nuclear magnetic resonance spectroscopy and simulated annealing-based calculations. Its three-dimensional structure was shown to be composed of two distinct domains, each of which is formed by a three-stranded antiparallel beta-sheet. Unexpectedly, BI-VI was found to share a similar folding and disulfide bond connectivities not with cystatin superfamily inhibitors which inhibit the same cysteine proteinases but with the Bowman-Birk trypsin/chymotrypsin inhibitor from soybean (BBI-I). BBI-I is a 71-residue inhibitor which has two independent inhibitory sites toward the serine proteinases trypsin and chymotrypsin. These structural similarities with BBI-I suggest that they have evolved from a common ancestor and differentiated in function during a course of molecular evolution." @default.
• W2040236473 created "2016-06-24" @default.
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• W2040236473 date "1996-01-01" @default.
• W2040236473 modified "2023-10-12" @default.
• W2040236473 title "Solution Structure of Bromelain Inhibitor VI from Pineapple Stem: Structural Similarity with Bowman−Birk Trypsin/Chymotrypsin Inhibitor from Soybean^," @default.
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• W2040236473 doi "https://doi.org/10.1021/bi952754+" @default.
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