title: Comparative membrane locations and activities of human monoamine oxidases expressed in yeast.
abstract: Human monoamine oxidases A and B were expressed under the control of a galactose inducible promoter in Saccharomyces cerevisiae. The two MAO isoenzymes were found located in the yeast mitochondrial outer membrane, probably in different orientations as suggested by controlled proteolysis experiments. A high level of both human MAO-A or -B activities is measured in intact mitochondria without the need for any detergent solubilisation step. The substrate and inhibitor selectivities of the membrane-bound MAOs are highly similar to those of purified human enzymes. The level of MAO-B activity, however, is selectively lowered when bound to the membrane.
authors.affiliation: Centre de Génétique Moléculaire du C.N.R.S., Laboratoire Propre Associé à l'Université Pierre-et-Marie-Curie, Gif-sur-Yvette, France.
authors.forename: P
authors.initials: P
authors.lastname: Urban
authors.forename: J K
authors.initials: JK
authors.lastname: Andersen
authors.forename: H P
authors.initials: HP
authors.lastname: Hsu
authors.forename: D
authors.initials: D
authors.lastname: Pompon
mesh_terms: D001483:Base Sequence; D003001:Cloning, Molecular; D003010:Clorgyline / Q000494:pharmacology; D004247:DNA; D006801:Humans; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000235:genetics / Q000378:metabolism*; D010293:Pargyline / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics* / Q000648:ultrastructure; D013379:Substrate Specificity
chemical_list: D004247:DNA; D010293:Pargyline; D008995:Monoamine Oxidase; D003010:Clorgyline