4. Dynamics of Enzyme Action

2018 ◽  
pp. 122-164
Keyword(s):  
1918 ◽  
Vol 33 (3) ◽  
pp. 453-462
Author(s):  
I.S. Falk ◽  
C.E.A. Winslow

1917 ◽  
Vol 31 (1) ◽  
pp. 97-123
Author(s):  
K.George Falk
Keyword(s):  

1915 ◽  
Vol 50 (2) ◽  
pp. 85-94 ◽  
Author(s):  
W. M. Bayliss
Keyword(s):  

1969 ◽  
Vol 47 (23) ◽  
pp. 4459-4466 ◽  
Author(s):  
J. Bryan Jones ◽  
Donald C. Wigfield

Determination of the activation parameters for the acid-, base-, and enzyme-catalyzed isomerizations of androst-5-ene-3,17-dione has revealed that the facility of the enzymic process is mainly due to an extremely low enthalpy of activation of 5.0 kcal mole−1. Further circumstantial evidence regarding the nature of the reacting groups at the active center has also been obtained, and a mechanism of enzyme action is proposed employing tyrosine and histidine as the principal amino acids responsible for catalyzing the isomerization.


The earlier experiments described by the writer upon the decomposition of glucose and mannitol by B. coli communis were open to the objection from the biological side that no attempt was made to distinguish those products which arose by enzyme action from those which might be more particularly associated in their formation with the growth and multiplication of the cells, and from the chemical side that certain substances of unknown composition, such as peptone, were employed, so that it was not possible to be sure that some of the products of fermentation had not been derived from this source. To overcome these objections the author has adopted a new plan of work which aims at separating the process of growth from that of fermentation.


1948 ◽  
Vol 1 (4) ◽  
pp. 319-326
Author(s):  
Gustav W. Rapp
Keyword(s):  

Science ◽  
1960 ◽  
Vol 131 (3393) ◽  
pp. 101-102
Author(s):  
Michael T. Ryan ◽  
C. A. Mavrides
Keyword(s):  

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