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首页> 外文期刊>Biochemistry >Active serine involved in the stabilization of the active site loop in the Humicola lanuginosa lipase
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Active serine involved in the stabilization of the active site loop in the Humicola lanuginosa lipase

机译：活性丝氨酸参与腐殖质脂酶中活性位点环的稳定化

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摘要

We have investigated the binding properties of and dynamics in Humicola lanuginosa lipase (HII) and the inactive mutant S146A (active Ser146 substituted with Ala) using fluorescence spectroscopy and molecular dynamics simulations, respectively. Hll and S146A show significantly different binding behavior for phosphatidylcholine (PC) and phosphatidylglycerol (PG) liposomes. Generally, higher binding affinity is observed for Hll than the S146A mutant. Furthermore,depending on the matrix, the addition of the transition state analogue benzene boronic acid increases the binding affinity of S146A, whereas only small changes are observed for I-Ill suggesting that the active site Lid in the latter opens more easily and hence more lipase molecules are bound to the liposomes. These observations are in agreement with molecular dynamics simulations and subsequent essential dynamics analyses. The results reveal that the hinges of the active site lid are more flexible in the wild-type Hll than in S146A. In contrast, larger fluctuations are observed in the middle region of the active site loop in S 146A than in Hll. These findings reveal that the single mutation (S146A) of the active site serine leads to substantial conformational alterations in the H. lanuginosa Lipase and different binding affinities. [References: 74]
机译：我们分别使用荧光光谱和分子动力学模拟研究了Humicola lanuginosa脂肪酶（HII）和无活性突变体S146A（用Ala取代的活性Ser146）的结合特性和动力学。 H11和S146A显示出对磷脂酰胆碱（PC）和磷脂酰甘油（PG）脂质体的显着不同的结合行为。通常，观察到对H11的结合亲和力高于S146A突变体。此外，取决于基质，过渡态类似物苯硼酸的添加增加了S146A的结合亲和力，而对I-III的观察到的变化很小，这表明后者中的活性位点Lid更容易打开，因此脂肪酶更多分子与脂质体结合。这些观察结果与分子动力学模拟和随后的基本动力学分析相符。结果表明，与S146A相比，在野生型H11中，活动部位盖的铰链更灵活。相反，在S 146A中在活动位点环的中间区域观察到的波动大于在H11中。这些发现表明，活性位点丝氨酸的单一突变（S146A）导致H.lanuginosa脂酶的实质构象改变和不同的结合亲和力。 [参考：74]

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