Molecular insights into mechanisms of lepidopteran serine proteinase resistance to natural plant defenses
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- 作者：Fá ; bio K. Tamaki ; Walter R. Terra ; warterra@iq.usp.br" class="auth_mail" title="E-mail the corresponding author
- 关键词：Insect-plant interaction ; Resistant serine-Proteinase ; Plant-proteinase inhibitors ; Ketone modification
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2015
- 出版时间：27 November 2015
- 年：2015
- 卷：467
- 期：4
- 页码：885-891
- 全文大小：1228 K
文摘
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Lepidopteran trypsins are more hydrophobic than coleopteran ones.
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Trypsin hydrophobicity-associated oligomerization seems to avoid plant inhibitors.
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Lepidopteran chymotrypsins have catalytic residues with high pKa.
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High pKa of catalytic residues are associated with ketone resistance.
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Structural features explain changes in properties of chymotrypsin catalytic residues.