Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone.
An enzyme which oxidizes aminoacetone to methylglyoxal has been purified from the particulate fraction of goat liver. Polyamines, such as spermidine and spermine, are also good substrates for this enzyme. The pH optimum for aminoacetone oxidation was found to be 8.2. The apparent Km values of the enzyme for aminoacetone and spermidine were 0.009 and 0.095 mM, respectively. The subunit molecular weight of the enzyme was 93,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The apparent molecular weight of the native enzyme was 186,000 by gel filtration. The enzyme is highly sensitive to carbonyl group reagents. The enzyme is not inhibited by monoamine and diamine oxidase inhibitors.
D000096:Acetone / Q000031:analogs & derivatives* / Q000378:metabolism; D000447:Aldehydes / Q000378:metabolism*; D006631:Amine Oxidase (Copper-Containing) / Q000037:antagonists & inhibitors; D000818:Animals; D006041:Goats; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008996:Monoamine Oxidase Inhibitors / Q000494:pharmacology; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D011765:Pyruvaldehyde / Q000378:metabolism*; D013379:Substrate Specificity; D000097667:Polyamine Oxidase
D000096:Acetone; D000447:Aldehydes; D006631:Amine Oxidase (Copper-Containing); D008996:Monoamine Oxidase Inhibitors; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011765:Pyruvaldehyde; D000097667:Polyamine Oxidase; C006495:aminoacetone