Vacuolar H+-pyrophosphatase

被引:381
作者
Maeshima, M [1 ]
机构
[1] Nagoya Univ, Grad Sch Bioagr Sci, Biochem Lab, Nagoya, Aichi 4648601, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2000年 / 1465卷 / 1-2期
关键词
cDNA; H+-pyrophosphatase; proton pump; vacuolar membrane; (plant);
D O I
10.1016/S0005-2736(00)00130-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The H+-translocating inorganic pyrophosphatase (H+-PPase) is a unique, electrogenic proton pump distributed among most land plants, but only some alga, protozoa, bacteria, and archaebacteria. This enzyme is a fine model for research on the coupling mechanism between the pyrophosphate hydrolysis and the active proton transport, since the enzyme consists of a single polypeptide with a calculated molecular mass of 71-80 kDa and its substrate is also simple. Cloning of the H+-PPase genes from several organisms has revealed the conserved regions that may be the catalytic site and/or participate in the enzymatic function. The primary sequences are reviewed with reference to biochemical properties of the enzyme, such as the requirement of Mg2+ and K+. In plant cells, H+-PPase coexists with H+-ATPase in a single vacuolar membrane. The physiological significance and the regulation of the gene expression of H+-PPase are also reviewed. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:37 / 51
页数:15
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