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Comparative membrane locations and activities of human monoamine oxidases expressed in yeast
Author(s) -
Urban P.,
Andersen J.K.,
Hsu H.-P.P.,
Pompon D.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80960-b
Subject(s) - yeast , biochemistry , membrane , saccharomyces cerevisiae , proteolysis , monoamine neurotransmitter , enzyme , chemistry , isozyme , substrate (aquarium) , galactose , biology , serotonin , receptor , ecology
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 membrane.