scholarly journals Questions in the Chemical Enzymology of MAO

Chemistry ◽  
2021 ◽  
Vol 3 (3) ◽  
pp. 959-978
Author(s):  
Rona R. Ramsay ◽  
Alen Albreht

We have structure, a wealth of kinetic data, thousands of chemical ligands and clinical information for the effects of a range of drugs on monoamine oxidase activity in vivo. We have comparative information from various species and mutations on kinetics and effects of inhibition. Nevertheless, there are what seem like simple questions still to be answered. This article presents a brief summary of existing experimental evidence the background and poses questions that remain intriguing for chemists and biochemists researching the chemical enzymology of and drug design for monoamine oxidases (FAD-containing EC 4.1.3.4).

2005 ◽  
Vol 35 (3) ◽  
pp. 189-193 ◽  
Author(s):  
Young-Kook KANG ◽  
Sang-Ho NAM ◽  
Hyung-Ok SOHN ◽  
Dong-Wook LEE

1981 ◽  
Vol 15 (6) ◽  
pp. 951-954 ◽  
Author(s):  
Bertha G. Ortega-Corona ◽  
José Carranza ◽  
Agustín Sosa ◽  
Patricia Guzmán-Amaya ◽  
Nora S. Esparza-Avalos ◽  
...  

1987 ◽  
Vol 7 (9) ◽  
pp. 701-704 ◽  
Author(s):  
Maitreyi Nag ◽  
Namita Nandi

Chloropromazine (CPZ) and imipramine at a concentration of 1×10−3 M inhibit rat brain mitochondrial monoamine oxidase activity in vitro by 70 and 55% respectively, while lithium, even at a concentration of 0.05 M, inhibits the activity of this enzyme very negligibly (4%). In vivo, these drugs at a dose level of 56 mg CPZ, 76 mg Jimipramine and 76 mg lithium chloride/Kg body wt., did not cause any observable variation from normal in brain mitochondrial monoamine oxidase activity.


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