College of Life Science and Biotechnology, Shanghai Jiaotong University, 800 Dongchuan Road, Shanghai 200240, China.
J Chem Inf Model. 2010 May 24;50(5):875-8. doi: 10.1021/ci900458u.
T1 lipase is isolated from the palm Geobacillus zalihae strain T1 in Malaysia, functioning as a secreted protein responsible for the catalyzing hydrolysis of long-chain triglycerides into fatty acids and glycerol at high temperatures. In the current study, using 30 ns molecular dynamics simulations at different temperatures, an aqueous activation was detected for T1 lipase. This aqueous activation in T1 lipase was mainly caused by a double-flap movement mechanism. The double flaps were constituted by the hydrophobic helices 6 and 9. Helix 6 employed two major components with the hydrophilic part at the surface and the hydrophobic part inside. In the aqueous solution, the hydrophobic part could provide enough power for helix 6 to move away, driving the protein into an open configuration and exposing the catalytic triad. Our findings could provide structural evidence to support the double-flap movement, revealing the catalytic mechanism for T1 lipase.
T1 脂肪酶从马来西亚的扎里亚氏芽孢杆菌菌株 T1 中分离出来，作为一种分泌蛋白，在高温下负责催化长链甘油三酯水解为脂肪酸和甘油。在本研究中，使用不同温度下的 30ns 分子动力学模拟，检测到 T1 脂肪酶的水相激活。T1 脂肪酶中的这种水相激活主要是由双瓣运动机制引起的。双瓣由疏水螺旋 6 和 9 组成。螺旋 6 由两个主要部分组成，亲水部分在表面，疏水部分在内部。在水溶液中，疏水部分可以为螺旋 6 的移动提供足够的动力，驱动蛋白质进入开放构象并暴露出催化三联体。我们的发现可以为双瓣运动提供结构证据，揭示 T1 脂肪酶的催化机制。
