Solution Kinetics of CC-1065 A-Ring Opening:  Substituent Effects and General Acid/Base Catalysis

2006 ◽  
Vol 128 (11) ◽  
pp. 3722-3727 ◽  
Author(s):  
Daniel V. LaBarbera ◽  
Edward B. Skibo
2011 ◽  
Vol 133 (13) ◽  
pp. 5124-5128 ◽  
Author(s):  
Jerry R. Mohrig ◽  
Nicholas J. Reiter ◽  
Randy Kirk ◽  
Michelle R. Zawadski ◽  
Nathan Lamarre-Vincent

Biochemistry ◽  
2003 ◽  
Vol 42 (27) ◽  
pp. 8298-8306 ◽  
Author(s):  
Paul A. Sims ◽  
Todd M. Larsen ◽  
Russell R. Poyner ◽  
W. Wallace Cleland ◽  
George H. Reed

1983 ◽  
Vol 213 (3) ◽  
pp. 603-607 ◽  
Author(s):  
C O'Fagain ◽  
B M Butler ◽  
T J Mantle

The effect of pH on the kinetics of rat liver arylsulphatases A and B is very similar and shows that two groups with pK values of 4.4-4.5 and 5.7-5.8 are important for enzyme activity. Substrate binding has no effect on the group with a pK of 4.4-4.5; however, the pK of the second group is shifted to 7.1-7.5 in the enzyme-substrate complex. An analysis of the effect of pH on the Ki for sulphate inhibition suggests that HSO4-is the true product. A model is proposed that involves the two ionizing groups identified in the present study in a concerted general acid-base-catalysed mechanism.


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