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Expression and inhibitory activity analysis of a 25-kD Bowman-Birk protease inhibitor in rice
Chen, J ; Mao, SJ ; Xie, Y ; Cao, ZR ; Zhang, Y ; Liu, J ; Chen, ZL ; Qu, LJ ; Gu, HY
刊名科学通报 英文版
2006
关键词Bowman-Birk inhibitor trypsin-inhibitory activity chymotrypsin-inhibitory activity disulfide bond AMINO-ACID-SEQUENCE REACTIVE-SITE LOOP TRYPSIN-INHIBITOR CRYSTAL-STRUCTURE CYCLIC-PEPTIDES CHYMOTRYPSIN SEEDS PROTEINASES RESOLUTION
DOI10.1007/s11434-005-0937-8
英文摘要Rice Bowman-Birk inhibitors (RBBI) with one (8 kD) or two homologous domains (16 kD) were found to be effective trypsin inhibitors in vitro. In this study, we demonstrate that the 25-kD protein corresponding to the three-domain RBBI indeed exists in rice in planta, and that the RBBIs are regulated by development and wounding. We also found by inhibitory activity assay that the 3:13 disulfide bond, but not the 4:5 disulfide bond, suppresses the trypsin-inhibitory activity, and the D3 domain of RBBI3-1 has no inhibitory activity against trypsin, chymotrypsin, paparin or subtilisin. Mutation analyses showed that conversion from Lys to Leu or Tyr in the N-terminal P1 site in D1 domain did not create chymotrypsin-inhibitory activity, suggesting that the structure of the reactive loop in D1 domain hinder the new inhibitory specificity at P1 site, and the chymotrypsin-inhibitory activity might need the participation of other structures, e.g. 3:13 disulfide bond.; Multidisciplinary Sciences; SCI(E); 8; ARTICLE; 1; 54-62; 51
语种英语
内容类型期刊论文
源URL[http://ir.pku.edu.cn/handle/20.500.11897/252554]  
专题生命科学学院
推荐引用方式
GB/T 7714
Chen, J,Mao, SJ,Xie, Y,et al. Expression and inhibitory activity analysis of a 25-kD Bowman-Birk protease inhibitor in rice[J]. 科学通报 英文版,2006.
APA Chen, J.,Mao, SJ.,Xie, Y.,Cao, ZR.,Zhang, Y.,...&Gu, HY.(2006).Expression and inhibitory activity analysis of a 25-kD Bowman-Birk protease inhibitor in rice.科学通报 英文版.
MLA Chen, J,et al."Expression and inhibitory activity analysis of a 25-kD Bowman-Birk protease inhibitor in rice".科学通报 英文版 (2006).
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