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具有氨基磷脂转运活性的P型ATP酶亚家族。

A subfamily of P-type ATPases with aminophospholipid transporting activity.

作者信息

Tang X, Halleck M S, Schlegel R A, Williamson P

机构信息

Department of Biology, Amherst College, MA 01002, USA.

出版信息

Science. 1996 Jun 7;272(5267):1495-7. doi: 10.1126/science.272.5267.1495.

DOI:10.1126/science.272.5267.1495
PMID:8633245
Abstract

The appearance of phosphatidylserine on the surface of animal cells triggers phagocytosis and blood coagulation. Normally, phosphatidylserine is confined to the inner leaflet of the plasma membrane by an aminophospholipid translocase, which has now been cloned and sequenced. The bovine enzyme is a member of a previously unrecognized subfamily of P-type adenosine triphosphatases (ATPases) that may have diverged from the primordial enzyme before the separation of the known families of ion-translocating ATPases. Studies in Saccharomyces cerevisiae suggest that aminophospholipid translocation is a general function of members of this family.

摘要

动物细胞表面磷脂酰丝氨酸的出现会引发吞噬作用和血液凝固。正常情况下,磷脂酰丝氨酸通过一种氨基磷脂转位酶被限制在质膜的内小叶,这种酶现已被克隆并测序。牛的这种酶是P型三磷酸腺苷酶(ATP酶)一个先前未被识别的亚家族的成员,该亚家族可能在已知的离子转运ATP酶家族分离之前就已从原始酶分化而来。对酿酒酵母的研究表明,氨基磷脂转位是该家族成员的一项普遍功能。

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