Deamination of aliphatic amines by monoamine oxidase A and B studied using a bioluminescence technique.
Deamination of n-octylamine and n-decylamine has been studied in various tissues using a new bioluminescence technique. Selectivity of n-octylamine and n-decylamine as substrates for monoamine oxidase (MAO) A or B has been determined using both clorgyline and (-)-deprenyl inhibition curves and kinetic parameters. Homogenates of rat brain, liver and heart containing predominantly MAO-A or -B were prepared by preincubation for 60 min with (-)-deprenyl or clorgyline (30 nM), respectively. Human placenta (MAO-A) and platelet (MAO-B) were used as reference tissues containing only one MAO form. In tissues (rat liver, brain) containing both MAO forms in equal proportion, inhibition curve studies showed a preference of both substrates for the B form of the enzyme; however, where MAO-A was the major form (rat heart, human placenta), clorgyline was the more effective inhibitor. In the beef brain cortex n-octylamine showed marked preference for MAO-B, whereas n-decylamine was selective toward-MAO-A. Kinetic studies in general supported the picture of greater selectivity of the aliphatic amine substrates for deamination by MAO-B, as reflected by lower Km values for this enzyme type. However, n-octylamine was more selective for MAO-B than n-decylamine in both kinetic and inhibition curve studies. The deamination of these aliphatic amine substrates cannot be explained only by reference to the binary classification of MAO into types A and B.
D000588:Amines / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008163:Luminescent Measurements; D008995:Monoamine Oxidase / Q000378:metabolism*; D008996:Monoamine Oxidase Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
D000588:Amines; D008996:Monoamine Oxidase Inhibitors; D008995:Monoamine Oxidase; C004744:decylamine; C008699:octylamine