Selective cleavage of pepsin by molybdenum metallopeptidase

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• 作者：Sudarat Yenjai ; Pinpinat Malaikaew ; Teerayuth Liwporncharoenvong ; Apinya Buranaprapuk ; ^{apinyac@swu.ac.th}
• 关键词：Cleavage reactions ; Proteins ; Molybdenum ; Protein&ndash ; metal interactions ; Transition metals
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：2 March, 2012
• 卷：419
• 期：1
• 页码：126-129
• 文件大小：339 K

摘要

In this study, the cleavage of protein by molybdenum cluster is reported for the first time. The protein target used is porcine pepsin. The data presented in this study show that pepsin is cleaved to at least three fragments with molecular weights of 鈭?3, 鈭?9 and 鈭?6 kDa when the mixture of the protein and ammonium heptamolybdate tetrahydrate ((NH₄)₆Mo₇O₂₄路4H₂O) was incubated at 37 掳C for 24 h. No self cleavage of pepsin occurs at 37 掳C, 24 h indicating that the reaction is mediated by the metal ions. N-terminal sequencing of the peptide fragments indicated three cleavage sites of pepsin between Leu 112-Tyr 113, Leu 166-Leu 167 and Leu 178-Asn 179. The cleavage reaction occurs after incubation of the mixture of pepsin and (NH₄)₆Mo₇O₂₄路4H₂O) only for 2 h. However, the specificity of the cleavage decreases when incubation time is longer than 48 h. The mechanism for cleavage of pepsin is expected to be hydrolytic chemistry of the amide bonds in the protein backbone.