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Inorganic pyrophosphatase
Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme () that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis, as well as other biochemical transformations.
==Structure==
Thermostable pyrophosphatase has been isolated from the extremophile ''Thermococcus litoralis''. The 3-dimensional structure was determined using x-ray crystallography, and was found to consist of two alpha-helices, as well as an antiparallel closed beta-sheet. The form of inorganic pyrophosphatase isolated from ''Thermococcus litoralis'' was found to contain a total of 174 amino acid residues and have a hexameric oligomeric organization (Image 1). Though the human form of the enzyme has not yet been isolated, a 1.23 kilobase cDNA segment has been identified that encodes a 32 kDa protein that is 94% identical to bovine inorganic pyrophosphatase. This DNA sequence has assigned to a gene locus on human chromosome 10.
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