Zwart K, Veenhuis M, van Dijken J P, Harder W
Arch Microbiol. 1980 Jun;126(2):117-26. doi: 10.1007/BF00511216.
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.
研究了甲胺作为非甲基营养型酵母产朊假丝酵母和甲基营养型酵母多形汉逊酵母生长氮源的代谢情况。两种微生物在含有葡萄糖和甲胺的培养基中生长与这些细胞中胺氧化酶的存在有关。该酶催化甲胺被分子氧氧化成氨、甲醛和过氧化氢，被认为是所研究生物体中甲胺代谢的关键酶。除了胺氧化酶的合成外，当将两种生物体的细胞从含有铵离子的培养基转移到以甲胺作为氮源的培养基中时，还观察到过氧化氢酶、甲醛和甲酸脱氢酶的去阻遏作用。酶的合成与细胞中一些大型微体的发育同时发生。细胞化学染色实验表明，两种生物体中胺氧化酶活性均位于微体中。在这些细胞器中也证明了过氧化氢酶活性，因此这些细胞器可被视为过氧化物酶体。本研究首次描述了过氧化物酶体胺氧化酶。
