Development of amine oxidase-containing peroxisomes in yeasts during growth on glucose in the presence of methylamine as the sole source of nitrogen.
The metabolism of methylamine as the nitrogen source for growth of the non-methylotrophic yeast Candida utilis and the methylotrophic yeast Hansenula polymorpha was investigated. Growth of both organisms in media with glucose and methylamine was associated with the presence of an amine oxidase in these cells. The enzyme catalyses the oxidation of methylamine by molecular oxygen into ammonia, formaldehyde and hydrogen peroxide and it is considered to be the key enzyme in methylamine metabolism in the organisms studied. In addition to synthesis of amine oxidase, derepression of catalase, formaldehyde and formate dehydrogenase was also observed upon transfer of cells of the two organisms from media containing ammonium ions into media containing methylamine as the nitrogen source. The synthesis of enzymes was paralleled by the development of a number of large microbodies in the cells. Cytochemical staining experiments indicated that the amine oxidase activity was located in the microbodies in both organisms. Catalase-activity was also demonstrated in these organelles, which can therefore be considered as peroxisomes. The present contribution is the first description of a peroxisomal amine oxidase.
D001203:Ascomycota / Q000648:ultrastructure*; D002175:Candida / Q000378:metabolism / Q000648:ultrastructure*; D002374:Catalase / Q000378:metabolism; D005613:Freeze Etching; D005947:Glucose / Q000378:metabolism*; D008744:Methylamines / Q000378:metabolism*; D008830:Microbodies / Q000201:enzymology / Q000648:ultrastructure; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism; D010843:Pichia / Q000378:metabolism / Q000648:ultrastructure*
D008744:Methylamines; D002374:Catalase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D005947:Glucose