caa a22 4500 46912170X CHVBK 20180323133140.0 cr unu---uuuuu 170328e19920201xx s 000 0 eng 10.1007/BF02246224 doi (NATIONALLICENCE)springer-10.1007/BF02246224 Molecular properties of monoamine oxidases A and B [Elektronische Daten] [Sau-Wah Kwan, J. Bergeron, C. Abell] Monoamine oxidases A and B (MAO-A and B) catalyze the oxidative catabolism of biogenic amines and xenobiotics. Investigation of these mitochondrial membrane proteins shows that they differ in substrate preference, inhibitor specificity, tissue and neuronal cell distribution, immunological properties, and nucleotide and deduced amino acid sequences. Comparisons of MAO-A and B from the human, bovine, and rat species show strikingly high similarity (85-88%) in the amino acid sequences of each enzyme. Furthermore, three regions in MAO-A and B have sequence identities across species of 78, 88, and 86%. These regions correspond to a nucleotide-binding site near the N-terminal end that is found in the vast majority of enzymes that require flavin adenine dinucleotide (FAD), a region of unknown function, and the FAD-binding site toward the C-terminal end. Genomic clones of MAO-B which span almost the entire gene (>40 kb) have been isolated, restriction mapped, and partially sequenced. Likewise, genomic clones of MAO-A that correspond to the 3′-flanking region have also been investigated. Current studies which focus on identification of the promotor and regulatory sequences should help to establish why MAO-A and B are localized in different subsets of neurons in brain. Springer-Verlag, 1992 MAO-A and B nationallicence cDNA sequences nationallicence Deduced amino acid sequences nationallicence Genomic clones nationallicence Restriction maps nationallicence Kwan Sau-Wah Division of Medicinal Chemistry, College of Pharmacy and Institute for Neuroscience, The University of Texas at Austin, 78712-1074, Austin, TX, USA aut Bergeron J. Division of Medicinal Chemistry, College of Pharmacy and Institute for Neuroscience, The University of Texas at Austin, 78712-1074, Austin, TX, USA aut Abell C. Division of Medicinal Chemistry, College of Pharmacy and Institute for Neuroscience, The University of Texas at Austin, 78712-1074, Austin, TX, USA aut Psychopharmacology Springer-Verlag 106(1992-02-01), S1-S5 0033-3158 106<S1 1992 106 213 https://doi.org/10.1007/BF02246224 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02246224 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kwan Sau-Wah Division of Medicinal Chemistry, College of Pharmacy and Institute for Neuroscience, The University of Texas at Austin, 78712-1074, Austin, TX, USA aut NATIONALLICENCE 700 1- Bergeron J. Division of Medicinal Chemistry, College of Pharmacy and Institute for Neuroscience, The University of Texas at Austin, 78712-1074, Austin, TX, USA aut NATIONALLICENCE 700 1- Abell C. Division of Medicinal Chemistry, College of Pharmacy and Institute for Neuroscience, The University of Texas at Austin, 78712-1074, Austin, TX, USA aut NATIONALLICENCE 773 0- Psychopharmacology Springer-Verlag 106(1992-02-01), S1-S5 0033-3158 106<S1 1992 106 213 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer