BIOCHEM 423 Chapter Notes - Chapter 8: Enzyme Kinetics, Menton, Reaction Rate Constant

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Enzymatic catalysis a reaction rate for a simple enzyme - catalysed. It we analyze the initial rate of an enzyme - catalyzed reaction and we assume that the. Chemical transformation of es to ep is rate - limiting ( kn > ) kz ) ts. Slowly consumed a the steady - state assumption proposes that the concentration of enzyme - substrate complex remains nearly constant through much of the reaction . Michaeli constant has unit of concentration a as a function of. Reactionary pouty k 5 es ] = km , v= vmax of a maximum value. Km is often associated with the attinity of enzyme for substrate under such conditions. Kcat < ( kt a km indicates the activity will be high when substrate at which the. Enzyme is above km . ( saturated a a 114 , a direct measure of the rate of product formation under optimum conditions . enzyme ) turnover number.