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首页> 外文期刊>Journal of bacteriology >The N-Terminal Propeptide of Vibrio vulnificus Extracellular Metalloprotease Is both an Inhibitor of and a Substrate for the Enzyme
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The N-Terminal Propeptide of Vibrio vulnificus Extracellular Metalloprotease Is both an Inhibitor of and a Substrate for the Enzyme

机译：创伤弧菌细胞外金属蛋白酶的N末端肽既是该酶的抑制剂又是该酶的底物。

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Vibrio vulnificus, a marine bacterium capable of causing wound infection and septicemia, secretes a 45-kDa metalloprotease (vEP) with many biological activities. The precursor of vEP consists of four regions: a signal peptide, an N-terminal propeptide (nPP), a C-terminal propeptide, and the mature protease. Two forms of vEP—vEP-45, which contains the mature protease plus the C-terminal propeptide, and vEP-34, which contains only the mature protease—were expressed in Escherichia coli and purified. vEP-45 and vEP-34 had similar activities with azocasein as a substrate, but vEP-34 had reduced activity toward insoluble proteins. The nPP of vEP was expressed as a His tag fusion protein, and its effect on vEP activity was investigated. nPP inhibited the activities of both vEP-45 and vEP-34 but not that of thermolysin, a different but related zinc-dependent protease. The inhibition of vEP by nPP was further examined using vEP-34 as a representative enzyme. The inhibition could be completely reversed under conditions of low enzyme and propeptide concentrations and with prolonged incubation, which resulted from the degradation of nPP by vEP. However, even at high nPP and vEP concentrations, inhibition of vEP by nPP at high temperatures was not effective, resulting in the degradation of both nPP and vEP. These results demonstrate that the nPP of vEP could bind to vEP and inhibit its activity, resulting in the degradation of the propeptide.
机译：能够引起伤口感染和败血病的海洋细菌 Viulio vulnificus 分泌具有许多生物学活性的45kDa金属蛋白酶（vEP）。 vEP的前体由四个区域组成：信号肽，N末端前肽（nPP），C末端前肽和成熟蛋白酶。在大肠杆菌中表达并纯化了两种形式的vEP，即含有成熟蛋白酶和C末端前肽的vEP-45和仅含有成熟蛋白酶的vEP-34。 vEP-45和vEP-34以偶氮酪蛋白为底物具有相似的活性，但vEP-34对不溶蛋白的活性降低。 vEP的nPP表示为His标签融合蛋白，并研究了其对vEP活性的影响。 nPP抑制vEP-45和vEP-34的活性，但不抑制嗜热菌蛋白酶的活性，后者是一种不同但相关的锌依赖性蛋白酶。使用vEP-34作为代表酶进一步检查了nPP对vEP的抑制作用。在低酶和前肽浓度的条件下，随着孵育时间的延长，抑制作用可以完全逆转，这是由于vEP降解nPP所致。但是，即使在高nPP和vEP浓度下，高温下nPP对vEP的抑制也无效，导致nPP和vEP均降解。这些结果表明，vEP的nPP可以与vEP结合并抑制其活性，从而导致前肽的降解。

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