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1996 (1)
1992 (1)
1Author    ErwinW. BeckerRequires cookie*
 Title    Dynamics and Kinetics of Enzymes Kinetic Equilibrium of Forces in Biochemistry  
 Abstract    To explain the high specificity, high reaction rate, and high thermodynamic efficiency in enzymatic processes, cooperation of the enzyme with a molecular transfer unit is assumed. A "kinetic equilibrium of forces" is suggested, which enables high reaction rates to occur under equilibrium conditions and a thorough examination of the substrate to be made without con­ sumption of free energy. In case o f ATPases, ion-binding proteins are the most probable trans­ fer units. By analyzing the elementary effect in muscle contraction it is shown that the new theorem may be of substantial value in elucidating biochemical processes. 
  Reference    Z. Naturforsch. 47c, 628—633 (1992); received May 18 1992 
  Published    1992 
  Keywords    Enzyme, Mechanism, Free Energy Transfer, ATPase, Calmodulin, Muscle Contraction 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0628.pdf 
 Identifier    ZNC-1992-47c-0628 
 Volume    47 
2Author    N. G. Faleev3, S. N. Spirina3, V. S. Ivoilov3, T. V. Dem, R. S. Phillips0Requires cookie*
 Title    The Catalytic Mechanism of Tyrosine Phenol-Lyase from Erwinia herbicola: The Effect of Substrate Structure on pH-Dependence of Kinetic Parameters in the Reactions with Ring-Substituted Tyrosines  
 Abstract    Apparently hom ogeneous tyrosine phenol-lyase (TPL) from Erwinia herbicola has been prepared by a new method. The pH -dependencies o f the main kinetic parameters for the reactions of Erwinia TPL with tyrosine, 2-fluorotyrosine, 3-fluorotyrosine, 2-chlorotyrosine, and 3.4-dihydroxyphenylalanine (D O P A) have been studied. The pattern of pH-dependence ° f V^max depends on the nature of the substituent in the aromatic ring. For the substrates bearing small substituents (H, 2-F, 3-F) Kmax values were found to be pH-independent. For 2-chlorotyrosine and DO PA Vmax decreased at lower pH, the effect being described by equa­ tion with one pKa. Generally two bases are reflected in the pH dependence of Vmax/K m. The first base, probably is responsible for the abstraction of a-proton, while the second one, interacts with the phenolic hydroxyl at the stage of binding. The reaction of TPL with DOPA differs from the reactions with other tyrosines by the requirement of an additional base which is reflected in the pH-profiles of both and VmaJ K m. For the reaction of TPL from Citrobacter intermedins with DO PA only Vma J K m values could be determined. The activity of Citrobacter enzyme towards DO PA is considerably less than that of E. herbicola enzyme, and its maximal value is attained at higher pH. 
  Reference    Z. Naturforsch. 51c, 363 (1996); received N ovem ber 22 1995/February 27 1996 
  Published    1996 
  Keywords    Tyrosine Phenol-Lyase, Mechanism, Kinetics, Substrate Structure, pH -Dependence 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0363.pdf 
 Identifier    ZNC-1996-51c-0363 
 Volume    51