Comparative membrane locations and activities of human monoamine oxidases expressed in yeast
- 29 July 1991
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 286 (1-2) , 142-146
- https://doi.org/10.1016/0014-5793(91)80960-b
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 mitochrondrial 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 mitochrondria 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 membraneKeywords
This publication has 23 references indexed in Scilit:
- Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FADBiochemical and Biophysical Research Communications, 1990
- Maximizing the expression of mammalian cytochrome P-450 monooxygenase activities in yeast cellsBiochimie, 1990
- Biochemistry and genetics of monoamine oxidasePharmacology & Therapeutics, 1990
- Expression of Functional Human Monoamine Oxidase A and B cDNAs in Mammalian CellsJournal of Neurochemistry, 1989
- Secondary structure determination for α‐neurotoxin from Dendroaspis polylepis polylepis based on sequence‐specific 1H‐nuclear‐magnetic‐resonance assignmentsEuropean Journal of Biochemistry, 1988
- cDNA cloning and functional expression in yeast Saccharomyces cerevisiae of β‐naphthoflavone‐induced rabbit liver P‐450 LM4 and LM6European Journal of Biochemistry, 1988
- Structural Features of Human Monoamine Oxidase A Elucidated from cDNA and Peptide SequencesJournal of Neurochemistry, 1988
- Selective inhibitors of monoamine oxidase A and B: Biochemical, pharmacological, and clinical propertiesMedicinal Research Reviews, 1984
- Comparative studies of purified and reconstituted monoamine oxidase from bovine liver mitochondriaBiochimica et Biophysica Acta (BBA) - Biomembranes, 1983
- [3H]HARMALINE AS A SPECIFIC LIGAND OF MAO A—I. PROPERTIES OF THE ACTIVE SITE OF MAO A FROM RAT AND BOVINE BRAINSJournal of Neurochemistry, 1979