运动发酵单胞菌的膜结合ATP酶；纯化与特性分析

Membrane-associated ATPase from Zymomonas mobilis; purification and characterization.

作者信息

Reyes L, Scopes R K

机构信息

Centre for Protein and Enzyme Technology, La Trobe University, Bundoora, Vic., Australia.

出版信息

Biochim Biophys Acta. 1991 Sep 30;1068(2):174-8. doi: 10.1016/0005-2736(91)90207-o.

DOI:10.1016/0005-2736(91)90207-o

PMID:1832963

Abstract

The major ATPase (adenosinetriphosphatase, EC 3.6.1.3) activity present in the membrane of Zymomonas mobilis has been isolated, using a novel combination of multifunctional hydrophobic adsorbents. On subjecting the preparation to gel filtration, activity was lost, but could be restored by reconstituting fractions from the column. Subunit composition of the fractions indicated that the Zymomonas mobilis ATPase is of the F0F1 type, and so is probably involved in proton pumping. The contribution of this ATPase to the overall ATP turnover in the cells has been calculated to be approximately 20% and so it may be partly responsible for the phenomenon of 'uncoupled growth' observed with Zymomonas mobilis.

摘要

运动发酵单胞菌细胞膜中存在的主要ATP酶（腺苷三磷酸酶，EC 3.6.1.3）活性已通过多功能疏水吸附剂的新型组合被分离出来。将该制剂进行凝胶过滤时，活性丧失，但通过重组柱中的组分可恢复活性。这些组分的亚基组成表明，运动发酵单胞菌ATP酶属于F0F1型，因此可能参与质子泵作用。据计算，这种ATP酶对细胞中总ATP周转的贡献约为20%，因此它可能部分导致了运动发酵单胞菌中观察到的“解偶联生长”现象。