Neurobiology 8. (2000)
1. szám - Research reports
Research report SEM ICA RB AZIDE-SENSITIVE AMINE OXIDASES: WIDESPREAD OCCURRENCE AND MANY NAMES AND FACES BOOMSMA, F. Department oflnternal Medicine 1, University Hospital Dijkzigt/Erasmus University, Rotterdam, The Netherlands Introduction In the past half century, amine oxidase activity has come to light in many different species: plants, microorganisms and animals, especially mammals. From the start the issue has been confused by the different methods used for determining the activity and by the differences in amines used as substrates. Accessability to the study of these enzymes has also been greatly hampered by the wide variation in nomenclature, which often involved the substrate used, the source of the enzyme activity, or both. Practically from the start various attempts have been made to provide a more rational approach to the study of these enzymes, based not only on substrates, but also on inhibitor profile and cofactor identity. Some excellent reviews have appeared (e.g. Buffoni, 1966; Blaschko, 1974). The most important step was made when it was realized that there were at least two different cofactors, with concomitant inhibitor profile, present. One group of amine oxidase enzymes depended for activity on a flavin adenine dinucleotide (FAD) cofactor, and was resistant to the action of carbonyl reagents. This group included the well-known monoamine oxidases (MAO) A and В and some polyamine oxidases, and has been classified as monoamine:oxygen oxidoreductase (deaminating) EC 1.4.3.4. The other group of amine oxidase enzymes appeared to have a carbonyl-containing cofactor, of uncertain identity, as a functional unit in the cofactor. The activity of this group of enzymes was not influenced by inhibitors of the FAD entity, but instead by compounds reacting with a carbonyl group, such as semicarbazide. This latter group, now classified as amineioxidoreductase (deaminating) ♦Presented at the 8th Amine Oxidase Workshop, Balatonőszöd, Hungary, 1998 1218-8068/00 $ 5.00 © 2000 Akadémiai Kiadó, Budapest Neurobiology 8 (1), pp. 1-16 (2000)