Abstract
Inorganic pyrophosphatases (sPPase; pyrophosphate phosphohydrolase, EC 3.6.1.1) are essential enzymes found in the cytosol and cellular organelles that drive anabolism through the hydrolysis of the energy-nch pyrophosphate (PPi) produced in the synthesis of biological polymers, making these processes thermodinamically irreversible. Since this hydrolysis replenishes Pi to the energy-converting systems, sPPases should play an important role in the intracellular “phosphate cycle”. In plants and some bacteria, sPPase also participates in sulfur metabolism by coupling PPi hydrolysis to sulfate activation steps. Moreover, PPi (like ATP) can be synthesized in photosynthetic bacteria as a result of photophosphorylation by a PPi-synthase [1].
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© 1998 Springer Science+Business Media Dordrecht
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Gómez, R., Löffelhardt, W., Losada, M., Serrano, A. (1998). Structural Diversity and Functional Conservation of Soluble Inorganic Pyrophosphatases from Photosynthetic Prokaryotes and Plastids. In: Garab, G. (eds) Photosynthesis: Mechanisms and Effects. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3953-3_858
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DOI: https://doi.org/10.1007/978-94-011-3953-3_858
Publisher Name: Springer, Dordrecht
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