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1Author    Paul RöschRequires cookie*
 Title    ,80-Exchange by Hydrolyzing Enzymes: Extension of the Model to Pi Molecules with Inequivalent Oxygen Atoms in the Bound State  
 Abstract    Enzymes causing an exchange o f oxygens from P\ with the surrounding water oxygens are very common. A statistical model for the data evaluation for an observation of this oxygen exchange by isotope methods is presented. It is shown how different cases o f inequivalence o f the four Pi oxygens may be uncovered. The number of reversals o f the oxygen exchange step on the enzyme and the apparent second order rate constant for the binding o f Pi to the enzyme are obtained as a result o f the data fitting procedure. Cobalt phosphatase, zinc phosphatase, and myosin subfragment 1 are treated as examples. 
  Reference    Z. Naturforsch. 36c, 539—544 (1981); received January 28/March 241981 
  Published    1981 
  Keywords    Enzyme Kinetics, ATPases, 31P-NMR, 180-Exchange, Enzyme Mechanism 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0539.pdf 
 Identifier    ZNC-1981-36c-0539 
 Volume    36