界面磷脂在磷脂酶A2催化中的双重作用。
Dual role of interfacial phospholipid in phospholipase A2 catalysis.
作者信息
Roberts M F, Deems R A, Dennis E A
出版信息
Proc Natl Acad Sci U S A. 1977 May;74(5):1950-4. doi: 10.1073/pnas.74.5.1950.
Abstract
The results of crosslinking experiments with dimethyl suberimidate and gel filtration binding studies are used to delineate a detailed model for phospholipase A2(phosphatide 2-acyl-hydrolase, EC 3.1.1.4) action in the presence of Ca2+ on mixed micelles of Triton X-100 and phospholipid. Important features of the "dual-phospholipid" model are: (i) the use of the nonionic surfactant as an inert matrix that may influence lipid conformation but does not interact with the enzyme; (ii) the involvement of two lipid molecules in a single cycle of catalysis as an explanation for the "surface dilution" phenomenon; (iii) the requirement of an ordered reaction whereby divalent metal ion binds prior to phospholipid binding; and (iv) the induction by lipid substrate of an asymmetric dimer structure for the enzyme.
摘要
使用亚辛二酸二甲酯交联实验结果和凝胶过滤结合研究来描绘磷脂酶A2（磷脂2-酰基水解酶，EC 3.1.1.4）在Ca2+存在下对Triton X-100和磷脂混合胶束作用的详细模型。“双磷脂”模型的重要特征包括：（i）使用非离子表面活性剂作为惰性基质，其可能影响脂质构象但不与酶相互作用；（ii）在单个催化循环中涉及两个脂质分子，作为对“表面稀释”现象的解释；（iii）需要有序反应，即二价金属离子在磷脂结合之前结合；以及（iv）脂质底物对酶的不对称二聚体结构的诱导。
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