The H+-Translocating ATPase in Vacuolar Membranes of Saccharomyces Cerevisiae
The H+-Translocating ATPase in Vacuolar Membranes of Saccharomyces Cerevisiae
复制标题
酿酒酵母液泡膜中的H-转位ATP酶
DOI：
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发表时间：
1985
期刊：
影响因子：
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通讯作者：
Y. Anraku
中科院分区：
文献类型：
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作者：
Y. Ohsumi;E. Uchida;Y. Anraku
用Ohsumi和Anraku（1981）的方法制备了纯化的正面朝外的液泡膜泡，研究了酿酒酵母液泡中H ~+-转运Mg ~（2+）-ATPase的性质。Cu ~（2+）和Zn ~（2+）离子对酶活性有抑制作用。最适pH为6.9。该酶依次水解ATP、GTP、UTP和CTP，测定ATP的Km值为0.2 mM，不水解ADP、腺苷-5 ′-基亚氨基二磷酸或对硝基苯基磷酸。ADP不抑制ATP被酶水解。
The properties of H+-translocating, Mg2+-ATPase in the vacuoles of Saccharomyces cerevisiae were studied, using purified right-side-out vacuolar membrane vesicles prepared by the method of Ohsumi and Anraku (1981).The enzyme requires Mg2+ ion but not Ca2+, K+, or Na+ ion. Cu2+ and Zn2+ ions inhibited the activity. The optimal pH is at pH 6.9. The enzyme hydrolyzes ATP, GTP, UTP, and CTP in this order and the Km value for ATP was determined as 0.2 mM. It does not hydrolyze ADP, adenosyl-5′-yl imidodiphosphate, or p-nitrophenyl phosphate. ADP does not inhibit hydrolysis of ATP by the enzyme.
粗糙脉孢菌液泡膜 ATP 酶与线粒体和质膜 ATP 酶的比较。
DOI：
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发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Bowman,EJ
通讯作者：
Bowman,EJ