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    Bioessays. 2008 Nov;30(11-12):1096-109.

    New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0).

    Source

    School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore. ggrueber@ntu.edu.sg

    Abstract

    Adenosine triphosphate, ATP, is the energy currency of living cells. While ATP synthases of archae and ATP synthases of pro- and eukaryotic organisms operate as energy producers by synthesizing ATP, the eukaryotic V-ATPase hydrolyzes ATP and thus functions as energy transducer. These enzymes share features like the hydrophilic catalytic- and the membrane-embedded ion-translocating sector, allowing them to operate as nano-motors and to transform the transmembrane electrochemical ion gradient into ATP or vice versa. Since archaea are rooted close to the origin of life, the A-ATP synthase is probably more similar in its composition and function to the "original" enzyme, invented by Nature billion years ago. On the contrary, the V-ATPases have acquired specific structural, functional and regulatory features during evolution. This review will summarize the current knowledge on the structure, mechanism and regulation of A-ATP synthases and V-ATPases. The importance of V-ATPase in pathophysiology of diseases will be discussed.

    PMID:
    18937357
    [PubMed - indexed for MEDLINE]

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