Isocitrate dehydrogenase from Azotobacter vinelandii. Order of substrate addition and product release

Biochemistry ◽  
1972 ◽  
Vol 11 (25) ◽  
pp. 4766-4778 ◽  
Author(s):  
Jeffrey S. Wicken ◽  
Albert E. Chung ◽  
James S. Franzen
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Azotobacter Vinelandii ◽  
Product Release ◽  
Substrate Addition

scholarly journals A catalytic mechanism for the enzyme benzylamine oxidase from pig plasma

1972 ◽  
Vol 130 (3) ◽  
pp. 713-728 ◽  
Author(s):  
C. E. Taylor ◽  
R. S. Taylor ◽  
C. Rasmussen ◽  
P. F. Knowles
Keyword(s):  
Catalytic Mechanism ◽  
Product Inhibition ◽  
Chemical Mechanism ◽  
Strictly Anaerobic ◽  
Anaerobic Conditions ◽  
Independent Evidence ◽  
Product Release ◽  
Benzylamine Oxidase ◽  
Inhibition Studies ◽  
Substrate Addition

Initial-velocity and product-inhibition studies on the enzyme benzylamine oxidase from pig plasma indicate that the order of substrate addition and product release is benzylamine on, ammonia off, oxygen on, hydrogen peroxide off, benzaldehyde off. Ammonia, but not benzaldehyde, is released under strictly anaerobic conditions which provides independent evidence for this order. Benzyl alcohol is a substrate for the enzyme. A chemical mechanism consistent with all the data is proposed.

A preliminary crystallographic study of isocitrate dehydrogenase from Azotobacter vinelandii

1977 ◽  
Vol 116 (1) ◽  
pp. 181-187 ◽  
Author(s):  
Edmund W. Czerwinski ◽  
Paul H. Bethge ◽  
F.Scott Mathews ◽  
Albert E. Chung
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Azotobacter Vinelandii ◽  
Crystallographic Study
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