Description
General description
Pyrophosphatase from E coli (E-PPase) has a broader pH optimum and contains four divalent cations per subunit. It comprises 175 amino acids with additional aspartate residue in the active site cavity. Structurally E-PPase is a homohexamer with six identical 20 kDa subunits. Magnesium is a cofactor for E-PPase.
Application
Pyrophosphatase, Inorganic from Escherichia coli has been used as a component of transcription buffer.
Inorganic pyrophosphatase (PPase) is a ubiquitous enzyme catalyzing the reaction PPi + H₂O → 2Pi.
It plays an important role in protein, RNA, and DNA synthesis.
Pyrophosphatase, inorganic from Escherichia coli has been used in assay for conjugation of ubiquitin and ubiquitin-like proteins. It has been used for one-pot three-enzyme system for synthesis of Lewis x and sialyl Lewis x antigens.
Biochem/physiol Actions
Pyrophosphatase from E coli (E-PPase) is an essential enzyme in yeast and bacteria The active site residues are crucial for binding to magnesium.
Physical form
Lyophilized powder in Tris-buffered salts containing protease inhibitors
Other Notes
A homohexameric protein containing 175 amino acid residues per subunit, its activity is Mg²⁺ dependent. It is a relatively thermostable protein.
One unit will release 1.0 μmole of inorganic orthophosphate per minute at pH 9 at 25 °C.
