Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
sodium/proton-translocating pyrophosphatase
The H+ pyrophosphatase is an transmembrane proton pump involved in establishing the H+ electrochemical potential difference between the vacuole lumen and the cell cytosol. Vacuolar-type H(+)-translocating inorganic pyrophosphatases have long been considered to be restricted to plants and to a few species of photo-trophic bacteria. However, in recent investigations, these pyrophosphatases have been found in organisms as disparate as thermophilic Archaea and parasitic protists [1]. [1]. 11335173. Vacuolar H(+) pyrophosphatases: from the evolutionary backwaters into the mainstream. Drozdowicz YM, Rea PA;. Trends Plant Sci 2001;6:206-211. (from Pfam)
sodium/proton-translocating pyrophosphatase such as K(+)-stimulated pyrophosphate-energized sodium pump and K(+)-insensitive pyrophosphate-energized proton pump, which utilize the energy of pyrophosphate hydrolysis as the driving force for sodium/proton movement across the membrane
V-type H(+)-translocating pyrophosphatase
This model describes proton pyrophosphatases from eukaryotes (predominantly plants), archaea and bacteria. It is an integral membrane protein and is suggested to have about 15 membrane spanning domains. Proton translocating inorganic pyrophosphatase, like H(+)-ATPase, acidifies the vacuoles and is pivotal to the vacuolar secondary active transport systems in plants.
sodium-translocating pyrophosphatase
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on