[Phosphorylation as a method of regulating inorganic pyrophosphatase activity in E. coli. II. Identification of the types of chemical bonds between phosphate and the enzyme].
A bond formed by phosphate with Pi-phosphorylated pyrophosphatase from E. coli was found to be labile in acidic and alkaline media and to be rapidly cleaved by hydroxylamine at neutral pH. N-Methylhydroxylamine modifies also activated carboxyl groups of the enzyme. Interaction of inorganic pyrophosphatase with ATP produces an alkali-resistant phosphoamide bond. A phosphorylated amino acid, identified as phosphohistidine, was isolated from the alkaline hydrolyzate of the ATP-phosphorylated pyrophosphatase.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D043564:Inorganic Pyrophosphatase; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation; D011755:Pyrophosphatases / Q000378:metabolism*
D010710:Phosphates; D000255:Adenosine Triphosphate; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase
Fosforilirovanie kak sposob reguliatsii aktivnosti neorganicheskoĭ pirofosfatazy E. coli. II. Identifikatsiia tipa khimicheskikh sviazeĭ fosfata s fermentom.