光合组织中油酸去饱和酶系统的酶的底物特异性。
Substrate specificities of the enzymes of the oleate desaturase system from photosynthetic tissue.
作者信息
Murphy D J, Woodrow I E, Mukherjee K D
出版信息
Biochem J. 1985 Jan 1;225(1):267-70. doi: 10.1042/bj2250267.
Abstract
In the microsomal fraction from young pea (Pisum sativum L.) leaves, the oleoyl moieties from oleoyl-CoA are principally transferred to the sn-2 position of phosphatidylcholine by oleoyl-CoA:1-acyl-lysophosphatidylcholine acyltransferase. The major product of this acyl transfer is 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine. The 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine is subsequently converted into 1-palmitoyl(stearoyl)-2-linoleoyl phosphatidylcholine by the oleate desaturase complex without equilibrating with the bulk membrane phosphatidylcholine pool. Hence, both the acyl transfer to phosphatidylcholine and the subsequent desaturation of oleoyl moieties occur on the sn-2 position of phosphatidylcholine, and there is also a functional coupling of the acyltransferase and oleate desaturase.
摘要
在嫩豌豆（豌豆）叶片的微粒体部分，油酰辅酶A中的油酰部分主要通过油酰辅酶A：1-酰基溶血磷脂酰胆碱酰基转移酶转移到磷脂酰胆碱的sn-2位。这种酰基转移的主要产物是1-棕榈酰（硬脂酰）-2-油酰磷脂酰胆碱。随后，1-棕榈酰（硬脂酰）-2-油酰磷脂酰胆碱在油酸去饱和酶复合物的作用下转化为1-棕榈酰（硬脂酰）-2-亚油酰磷脂酰胆碱，而不与整体膜磷脂酰胆碱池达到平衡。因此，酰基向磷脂酰胆碱的转移以及随后油酰部分的去饱和都发生在磷脂酰胆碱的sn-2位，并且酰基转移酶和油酸去饱和酶之间也存在功能偶联。
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本文引用的文献
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