326 



Enzyme Kinetics of Hydrolytic Reactions / 1 "7 : 3 



K„/xq = 0.5 e/xQ = 0.01 k 7 = 

 l.0 t h i i J i i +. 



53 





Note large discrepancies for 7"<3. These, however , 

 /jove ///Afe effect on values for 7">5. 



(a) 



Qj 

 I 



I 



Approximation 



• i/x 



o p/e 



o l//(A,xJ) 



600 



i4s o£ove Zx// with a different time base. 



(b) 



Figure 6. Exact and approximate solutions of Michaelis- 

 Menten equations for hydrolase kinetics. Lines show exact 

 values computed with electronic digital computer. Points 

 labeled show values predicted by the approximation. 



knows, it is always best to plot a straight line graph. By taking recipro- 

 cals in Equation 12a, one obtains 



1_ 



V 



1 



max 



1 + 



K 



M 



(12b) 



A graph of 1 / V against 1 \x is a straight line ; it is known as a Lineweaver- 

 Burk plot. Figure 7a illustrates in this fashion that sucrase does obey 

 Michaelis-Menten kinetics. A better form is obtained by multiplying 

 both sides of Equation 12b by x, giving 



J- [* + Km] (12c) 



x 

 V 



max 



