Structural basis for the reversibility of proton pyrophosphatase.

Proton Pyrophosphatase (H-PPase) is an evolutionarily conserved enzyme regarded as a bona fide vacuolar marker. However, H-PPase also localizes at the plasma membrane of the phloem, where, evidence suggests that it functions as a Pyrophosphate Synthase and participates in phloem loading and photosynthate partitioning. We believe that this pyrophosphate synthesising function of H-PPase is fundamentally rooted to its molecular structure, and here we postulate, on the basis of published crystal structures of membrane-bound pyrophosphatases, a plausible mechanism of pyrophosphate synthesis.