Abstract
Nearly 200 anabolic reactions liberate pyrophosphate (PPi), a byproduct of NTP hydrolysis (Kornberg, 1962; Maeshima, 2000; Heinonen, 2001; Ferjani et al., 2014a,b). In living cells, PPi must be hydrolyzed to orthophosphate by pyrophosphatase (PPase), because it suppresses the above reactions. PPases fall into two major classes, soluble PPases (sPPases) and membrane-bound H+-PPases (H+-PPases). In plants, vacuolar H+-PPase uses the energy released by PPi hydrolysis to acidify the vacuole, and its activity is particularly high in young tissues (Martinoia et al., 2007). Nevertheless, the physiological roles of PPases remain unclear due to severe phenotypes in loss-of-function mutants in various organisms (Ferjani et al., 2011 and references therein). Due to the importance of PPi homeostasis for life, this paper presents the most recent findings in this field and discusses the present situation along with future directions.
Highlights
200 anabolic reactions liberate pyrophosphate (PPi), a byproduct of NTP hydrolysis (Kornberg, 1962; Maeshima, 2000; Heinonen, 2001; Ferjani et al, 2014a,b)
Vacuolar H+-PPase uses the energy released by PPi hydrolysis to acidify the vacuole, and its activity is high in young tissues (Martinoia et al, 2007)
Due to the importance of PPi homeostasis for life, this paper presents the most recent findings in this field and discusses the present situation along with future directions
Summary
200 anabolic reactions liberate pyrophosphate (PPi), a byproduct of NTP hydrolysis (Kornberg, 1962; Maeshima, 2000; Heinonen, 2001; Ferjani et al, 2014a,b). PPi must be hydrolyzed to orthophosphate by pyrophosphatase (PPase), because it suppresses the above reactions. Vacuolar H+-PPase uses the energy released by PPi hydrolysis to acidify the vacuole, and its activity is high in young tissues (Martinoia et al, 2007).
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