[Functionally important lysine residues in inorganic pyrophosphatase from E. coli. II. Isolation and characteristics of modified tryptic peptide and analysis of the functional role of lysine residues controlling enzyme activity].
Inactivation of inorganic pyrophosphatase from E. coli by pyridoxal-5'-phosphate is due to the modification of a lysine residue located in the tryptic peptide with the Asp-Leu-Pro-Glu N-terminal sequence. In course of the enzymatic process this lysine-residue appears to be in the protonated state and either operators as the proton donor for the product of the enzymatic reaction or is involved in stabilization of the transition state.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002131:Calcium Pyrophosphate / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D043564:Inorganic Pyrophosphatase; D007700:Kinetics; D008239:Lysine / Q000378:metabolism*; D046911:Macromolecular Substances; D009842:Oligopeptides / Q000302:isolation & purification*; D011732:Pyridoxal Phosphate / Q000378:metabolism; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism
D046911:Macromolecular Substances; D009842:Oligopeptides; D011732:Pyridoxal Phosphate; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase; D008239:Lysine; D002118:Calcium; D002131:Calcium Pyrophosphate
Funktsional'no vazhnyĭ ostatok lizina v neorganicheskoĭ pirofosfataze iz E. coli. II. Vydelenie i kharakteristika modifitsirovannogo tripticheskogo peptida i issledovanie funktsional'noĭ roli ostatka lizina, kontroliruiushchego fermentativnuiu aktivnost'.