ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE-BINDING SITE IN CANDIDA-RUGOSA LIPASE
ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE-BINDING SITE IN CANDIDA-RUGOSA LIPASE
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DOI：
10.1021/bi00178a005
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发表时间：
1994-03-29
期刊：
影响因子：
2.9
通讯作者：
CYGLER, M
中科院分区：
文献类型：
--
作者：
GROCHULSKI, P;BOUTHILLIER, F;CYGLER, M
皱褶假丝酵母脂肪酶抑制剂复合物的结构表明，易切断的脂肪酰基链被束缚在一个狭窄的，疏水的隧道，这是唯一的脂肪酶研究到目前为止。甘油三酯结合的建模表明，结合脂质必须采用“音叉”构象。的配合物，类似物的反应途径的酰化和脱酰化步骤的四面体中间体，本地化的含氧阴离子孔的组件，并定义酯水解的立体化学。与其他脂肪酶的比较表明，易切断的脂肪酰基链和酯键的定位和水解的立体化学是相同的，在所有的脂肪酶共享的α/β-水解酶折叠。
The structures of Candida rugosa lipase-inhibitor complexes demonstrate that the scissile fatty acyl chain is bound in a narrow, hydrophobic tunnel which is unique among lipases studied to date. Modeling of triglyceride binding suggests that the bound lipid must adopt a ''tuning fork'' conformation. The complexes, analogs of tetrahedral intermediates of the acylation and deacylation steps of the reaction pathway, localize the components of the oxyanion hole and define the stereochemistry of ester hydrolysis. Comparison with other lipases suggests that the positioning of the scissile fatty acyl chain and ester bond and the stereochemistry of hydrolysis are the same in all lipases which share the alpha/beta-hydrolase fold.