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凡纳滨对虾蛋白酶激活巯基还原化合物的机制。

Penaeus vannamei protease activating mechanism of sulfhydryl reducing compounds.

机构信息

Department of Marine Biology, Faculty of Sciences, University of Hormozgan, Bandar Abbas, Iran.

Department of Biochemistry, Faculty of Sciences, University of Hormozgan, Bandar Abbas, Iran.

出版信息

Int J Biol Macromol. 2018 Jun;112:1131-1137. doi: 10.1016/j.ijbiomac.2018.02.087. Epub 2018 Feb 15.

Abstract

For the very first time, protease enzyme from Penaeus vannamei was investigated for its activation with thiol reductant compounds. The mechanism by which sulfhydryl reductant compounds enhances the activity of P. vannamei protease still remains unclear. In this study, it was discovered that thiol-reactive compounds increase P. vannamei protease activity by a factor of about 4 with increasing V and decreasing Km parameters. Moreover, the reaction is an S2-type that does not require the initial binding of the thiol group of these compounds to the enzyme. Additionally, k increased appreciably with increasing concentration of sulfhydryl reductant compounds. The linearity of this plot indicates that k is unaffected by the addition of thiol compounds. Hence, the observed effect of thiol compounds on K seems to be due to an increase in k. These results suggest that the activation mechanism of P. vannamei protease almost certainly takes place by an S2 reaction mechanism.

摘要

这是首次研究凡纳滨对虾蛋白酶的巯基还原剂化合物的激活作用。巯基还原剂化合物增强凡纳滨对虾蛋白酶活性的机制尚不清楚。在本研究中,发现巯基反应性化合物可使凡纳滨对虾蛋白酶的活性增加约 4 倍,同时 V 值增加,Km 值降低。此外,该反应是 S2 型,不需要这些化合物的巯基基团与酶的初始结合。此外,随着巯基还原剂化合物浓度的增加,k 值显著增加。该线性图表明,k 值不受添加巯基化合物的影响。因此,观察到的巯基化合物对 K 的影响似乎是由于 k 的增加所致。这些结果表明,凡纳滨对虾蛋白酶的激活机制几乎肯定是通过 S2 反应机制发生的。

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