胰腺磷脂酶A2的位点特异性ε-NH2单酰化。1. 制备与性质
Site-specific epsilon-NH2 monoacylation of pancreatic phospholipase A2. 1. Preparation and properties.
作者信息
Van der Wiele F C, Atsma W, Dijkman R, Schreurs A M, Slotboom A J, De Haas G H
机构信息
Laboratory of Biochemistry, State University of Utrecht, Transitorium III, University Center De Uithof, The Netherlands.
出版信息
Biochemistry. 1988 Mar 8;27(5):1683-8. doi: 10.1021/bi00405a045.
The lipid-binding domain of pancreatic phospholipases A2 contains a number of exposed, hydrophobic amino acid side chains that are involved in the binding of the enzyme to organized lipid-water interfaces. Besides these apolar residues, at least two positively charged lysine groups are present in positions 10 and 116 of the lipid-binding domain. In order to investigate the possible function of these basic side chains in the lipid-binding process, a number of specifically acylated enzyme mutants were prepared, and their kinetic and lipid-binding properties have been compared with those of the native enzymes. It is concluded that the attachment of a long-chain acyl group in an amide linkage to Lys10 or Lys116 phospholipase A2 has only a minor influence on the catalytic properties of the enzyme. On the other hand, the lipid-binding properties of the mutant enzymes appear to be considerably reinforced.
胰腺磷脂酶A2的脂质结合结构域包含许多暴露的疏水氨基酸侧链，这些侧链参与酶与有序脂质-水界面的结合。除了这些非极性残基外，脂质结合结构域的第10位和第116位至少存在两个带正电荷的赖氨酸基团。为了研究这些碱性侧链在脂质结合过程中可能的功能，制备了一些特定酰化的酶突变体，并将它们的动力学和脂质结合特性与天然酶进行了比较。得出的结论是，长链酰基以酰胺键连接到磷脂酶A2的Lys10或Lys116上，对酶的催化特性只有轻微影响。另一方面，突变酶的脂质结合特性似乎得到了显著增强。
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