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J Bacteriol. 2012 Sep;194(17):4546-9. doi: 10.1128/JB.00714-12. Epub 2012 Jun 22.

本文引用的文献

1
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.钠离子转运型V-ATP酶转子环的离子结合与选择性
Proc Natl Acad Sci U S A. 2008 Jun 24;105(25):8607-12. doi: 10.1073/pnas.0800992105. Epub 2008 Jun 16.
2
Deletion analysis of the subunit genes of V-type Na+-ATPase from Enterococcus hirae.平肠球菌V型钠-ATP酶亚基基因的缺失分析
J Biochem. 2006 Jun;139(6):1045-52. doi: 10.1093/jb/mvj108.
3
Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.来自平肠球菌的V型钠-ATP酶转子的结构。
Science. 2005 Apr 29;308(5722):654-9. doi: 10.1126/science.1110064. Epub 2005 Mar 31.
4
Arginine residue at position 573 in Enterococcus hirae vacuolar-type ATPase NtpI subunit plays a crucial role in Na+ translocation.平肠球菌液泡型ATP酶NtpI亚基中第573位的精氨酸残基在钠离子转运中起关键作用。
J Biol Chem. 2002 Jul 5;277(27):24405-10. doi: 10.1074/jbc.M200973200. Epub 2002 Apr 30.
5
ATP-dependent affinity change of Na+-binding sites of V-ATPase.
J Biol Chem. 2001 Dec 21;276(51):48337-40. doi: 10.1074/jbc.M106821200. Epub 2001 Sep 13.
6
Indispensable glutamic acid residue-139 of NtpK proteolipid in the reaction of vacuolar Na(+)-translocating ATPase in Enterococcus hirae.
Biosci Biotechnol Biochem. 1999 Jun;63(6):1125-9. doi: 10.1271/bbb.63.1125.
7
Enterococcus hirae vacuolar ATPase is expressed in response to pH as well as sodium.
FEBS Lett. 1999 Jul 2;454(1-2):67-70. doi: 10.1016/s0014-5793(99)00776-0.
8
Properties of the V0V1 Na+-ATPase from Enterococcus hirae and its V0 moiety.
J Biochem. 1999 Feb;125(2):414-21. doi: 10.1093/oxfordjournals.jbchem.a022302.
9
Structure, function and regulation of the vacuolar (H+)-ATPase.液泡（H⁺）-ATP酶的结构、功能及调节
Annu Rev Cell Dev Biol. 1997;13:779-808. doi: 10.1146/annurev.cellbio.13.1.779.
10
Purification and reconstitution of Na+-translocating vacuolar ATPase from Enterococcus hirae.来自平肠球菌的 Na⁺转运液泡 ATP 酶的纯化与重组。
J Biol Chem. 1997 Oct 3;272(40):24885-90. doi: 10.1074/jbc.272.40.24885.

谷氨酸 139 残基在 V 型 Na+-ATP 酶 NtpK 亚基的催化周转中与屎肠球菌耐盐性的关系。

Significance of the glutamate-139 residue of the V-type Na+-ATPase NtpK subunit in catalytic turnover linked with salt tolerance of Enterococcus hirae.

机构信息

Integrated Center for Sciences, Ehime University, Matsuyama, Japan1; Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.

出版信息

J Bacteriol. 2011 Jul;193(14):3657-61. doi: 10.1128/JB.01537-10. Epub 2011 May 20.

DOI:10.1128/JB.01537-10
PMID:21602356
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3133306/
Abstract

A Glu139Asp mutant of the NtpK subunit (kE139D) of Enterococcus hirae vacuolar-type ATPase (V-ATPase) lost tolerance to sodium but not to lithium at pH 10. Purified kE139D V-ATPase retained relatively high specific activity and affinity for the lithium ion compared to the sodium ion. The kE139 residue of V-ATPase is indispensable for its enzymatic activity that is linked with the salt tolerance of enterococci.

摘要

A Glu139Asp mutant of the NtpK subunit (kE139D) of Enterococcus hirae vacuolar-type ATPase (V-ATPase) lost tolerance to sodium but not to lithium at pH 10. Purified kE139D V-ATPase retained relatively high specific activity and affinity for the lithium ion compared to the sodium ion. The kE139 residue of V-ATPase is indispensable for its enzymatic activity that is linked with the salt tolerance of enterococci.

中文译文

耐辐射球菌液泡型 ATP 酶（V-ATPase）NtpK 亚基的 Glu139Asp 突变体（kE139D）在 pH 值为 10 时对钠离子失去耐受性，但对锂离子仍有耐受性。与钠离子相比，纯化的 kE139D V-ATPase 对锂离子仍保持着相对较高的比活度和亲和力。V-ATPase 的 kE139 残基对于与肠球菌耐盐性相关的其酶活性是不可或缺的。