TY  - BOOK
AU  - Baltscheffsky,M.
AU  - Schultz,A.
AU  - Baltscheffsky,H.
TI  - H.-proton-pumping inorganic pyrophosphatase: a tightly membrane-bound family
KW  - H.-PROTON-PUMPING INORGANIC PYROPHOSPHATASE
KW  - H.-PROTON-PUMPING INORGANIC PYROPHOSPHATE SYNTHASE
KW  - H.-ATPASE
KW  - H.-ATP SYNTHASE
KW  - AMINO ACID SEQUENCE
KW  - EVOLUTION
KW  - ENZYME FAMILY
N2  - The earliest known H+-proton-pumping inorganic pyrophosphatase, the integrally membrane-bound H+-protonpumping inorganic pyrophosphate synthase from Rhodospirillum rubrum, is still the only alternative to H+-ATP synthase in biological electron transport phosphorylation. Cloning of several higher plant vacuolar H+-proton-pumping inorganic pyrophosphatase genes has led to the recognition that the corresponding proteins form a family of extremely similar proton-pumping enzymes. The bacterial H+-proton-pumping inorganic pyrophosphate synthase and two algal vacuolar H+-proton-pumping inorganic pyrophosphatases are homologous with this family, as deduced from their cloned genes. The prokaryotic and algal homologues differ more than the H+-proton-pumping inorganic pyrophosphatases from higher plants, facilitating recognition of functionally significant entities. Primary structures of H+- proton-pumping inorganic pyrophosphatases are reviewed and compared with H+-ATPases and soluble proton-pumping inorganic pyrophosphatases
UR  - https://drive.google.com/file/d/1RYlPQ2iM4UE6yeqozv1iMBym1cLY_jik/view?usp=drivesdk
ER  -