H+‐proton‐pumping inorganic pyrophosphatase: a tightly membrane‐bound family

FEBS Letters

Baltscheffsky, Herrick¹  Baltscheffsky, Margareta¹  Schultz, Anders¹ 

[1] Department of Biochemistry, Arrhenius Laboratories, Stockholm University, S-106 91 Stockholm, Sweden

关键词: H+-proton-pumping inorganic pyrophosphatase;    H+-proton-pumping inorganic pyrophosphate synthase;    H+-ATPase;    H+-ATP synthase;    Amino acid sequence;    Evolution;    Enzyme family;    PPi;    inorganic pyrophosphate;    PPase;    inorganic pyrophosphatase;    ATP;    adenosine triphosphate;    ATPase;    adenosine triphosphatase;   

DOI  :  10.1016/S0014-5793(99)00617-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The earliest known H⁺-proton-pumping inorganic pyrophosphatase, the integrally membrane-bound H⁺-proton-pumping 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.

【 授权许可】

Unknown