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.
Read more about this topic: Inorganic Pyrophosphatase
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