title: [Functionally important lysine residues in inorganic pyrophosphatase from E. coli. I. Interaction of inorganic pyrophosphatase with pyridoxal-5'-phosphate].
abstract: Interaction of inorganic pyrophosphatase from E. coli with pyridoxal-5'-phosphate includes binding of the reagent at the active site through the phosphate group and then a reversible modification of one lysine residue in each of the enzyme's subunit. In the equilibrium state the protein's molecules contain both inactive modified and native subunits. A stable secondary amine is formed upon the sodium borohydride reduction of the modified protein.
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D043564:Inorganic Pyrophosphatase; D007700:Kinetics; D008239:Lysine / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*
chemical_list: D011732:Pyridoxal Phosphate; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase; D008239:Lysine
vernacular_title: Funktsional'no vazhnyĭ ostatok lizina v neorganicheskoĭ pirofosfataze iz E. coli. I. Vzaimodeĭstvie neorganicheskoĭ pirofosfatazy s piridoksal'-5'-fosfatom.