Abstract:
: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.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Zwart K,Veenhuis M,van Dijken JP,Harder Wdoi
10.1007/BF00511216subject
Has Abstractpub_date
1980-06-01 00:00:00pages
117-26issue
2eissn
0302-8933issn
1432-072Xjournal_volume
126pub_type
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