Inorganic pyrophosphatase--II. Purification and studies of some properties of the enzyme isolated from thermophylic bacterium Thermus flavus 70 K.
Inorganic pyrophosphatase was isolated from T. flavus in a homogeneous form with a specific activity of 400 U/mg. The enzyme has an isoelectric point 5.0 and consists of 4 subunits each of 24,000 mol. wt. Pyrophosphatase possesses high thermal stability. The enzyme can hydrolyze PPi, ATP and p-nitrophenylphosphate. Kinetic constants of the enzyme's interaction with the metal-activator and metal-substrate complex have been estimated.
D055598:Chemical Phenomena; D002621:Chemistry; D004589:Electrophoresis, Disc; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D043564:Inorganic Pyrophosphatase; D007700:Kinetics; D008956:Models, Chemical; D011755:Pyrophosphatases / Q000302:isolation & purification*; D013379:Substrate Specificity; D013824:Thermus / Q000201:enzymology*
D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase