Transport adenosine triphosphatases: properties and functions.
Transport adenosine triphosphatases: properties and functions.
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转运三磷酸腺苷酶：性质和功能。
DOI：
10.1152/physrev.1981.61.1.1
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发表时间：
1981
影响因子：
33.6
通讯作者：
Sjoerd L. Bonting
中科院分区：
文献类型：
--
作者：
F. S. Stekhoven;Sjoerd L. Bonting
本文综述了具有转运功能的膜上atp酶。这些酶的一个共同特点是它们可以分析相同的东西。利用整个反应（ATP水解为ADP和无机磷酸盐），并利用该反应的自由能变化，在离子所在的膜上沿电化学梯度进行离子运输。它们是载体酶，因为它们的酶活性导致离子在膜上沿一定方向运输。最著名的转运atp酶的例子是Na+和K+激活的atp酶（Na-K- atp酶）和Ca2+和Mg2+激活的atp酶（ca - mg - atp酶）。Na-K- atp酶，由Skou（340）于1957年发现)运输Na+和K+。1961年，Hasselbach和Makinose（120）在肌肉肌浆网中发现了ca - mg - atp酶，1966年，Schatzmann（296）在红细胞膜中发现了ca - mg - atp酶，它在红细胞膜中运输Ca2+离子。1965年，Durbin和Kasbekar（67）报道阴离子敏感的atp酶是一种转运碳酸氢盐和氯化物的atp酶。K+激活的atp酶（kh - atp酶），最早由Forte等人（80）于1967年描述为K+激活的磷酸酶活性，似乎在胃粘膜分泌氢离子中起作用。到目前为止，还没有发现转运atp酶在非离子转运中起直接作用。关于Na+-K+-ATPase系统（31，X, 90,102,155, 170,272,313,344,347,415）和Ca2+-Mg2+-ATPase系统（54,117-119,298,359）的一些综述已经发表。对阴离子敏感的atp酶有一个简单的综述（336），最近三篇关于胃酸分泌的综述讨论了kh - atp酶（285,290,291）。对所有已知转运atp酶的综合综述，描述它们的共同特征和差异，是罕见的（33,251）。
This review deal s with membrane-located ATPases that have a transport function. A common characteristic of these enzymes is that they ca talyze the sam. e overall reaction (the hydrolysis of ATP to ADP and inorganic phosphate) and utilize the free energy change of this reaction for the transport of ions against an electrochemical gradient across the membrane in which they are located. They are vectorial enzymes, in that their enzymatic activity leads to the transport of an ion in a certain direction across a membrane. The best-known examples of the transport ATPases are the Na+-and K+-activated ATPase (Na-K-ATPase) and the Ca2+-and Mg2+-activated ATPase (Ca-Mg-ATPase). The Na-K-ATPase, discovered in 1957 by Skou (340)) transports Na+ and K+. The Ca-Mg-ATPase was discovered in 1961 by Hasselbach and Makinose (120) in muscle sarcoplasmic reticulum and in 1966 by Schatzmann (296) in erythrocyte membrane, where it transports Ca2+ ions. The anion-sensitive ATPase was reported in 1965 by Durbin and Kasbekar (67) to be a transport ATPase for bicarbonate and chloride. The K+-activated ATPase (KH-ATPase), first described as a K+-activated phosphatase activity by Forte et al.(80) in 1967, appears to play a role in hydrogen ion secretion by the gastric mucosa. So far no transport ATPases have been found that play a direct role in nonionic transport.Several reviews covering certain aspects of the Na+-K+-ATPase system (31, X, 90,102,155, 170,272,313,344,347,415) and the Ca2+-Mg2+-ATPase system (54, 117-119, 298, 359) have been published. A brief review on anion-sensitive ATPase is available (336), and the KH-ATPase is discussed in three recent reviews on gastric acid secretion (285, 290, 291). Integrated reviews on all known transport ATPases, describing both their common features and their differences, are rare (33, 251).