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  • Catalase  (3)
  • Acyl-CoA synthetase  (1)
  • Corynebacterium simplex, Production of Co-Coproporphyrin, Utilization of Hydrocarbon  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 97 (1974), S. 259-271 
    ISSN: 1432-072X
    Keywords: Corynebacterium simplex, Production of Co-Coproporphyrin, Utilization of Hydrocarbon ; Cobalt-Coproporphyrin III, Production by Corynebacterium simplex ; Utilization of Hydrocarbon by Corynebacterium simplex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A vitamin B12-producing and hydrocarbon-utilizing bacterium, Corynebacterium simplex, accumulated an appreciable amount of cobalt-porphyrin in cultural filtrates when grown on a n-hexadecane medium containing sufficient amounts of cobaltous sulfate and an appropriate detergent. When grown without the detergent, the cobalt-porphyrin was found only in the cells of the organism. In the latter case, the content of cobalt-porphyrin was comparable to that of vitamin B12 and 7 times lower than that of iron-porphyrin. Though the organism required cobaltous sulfate for optimal growth, the requirement could be efficiently replaced by the supplementation of cobalt-porphyrin and partly of vitamin B12. The porphyrin moieties of extra- and intracellular cobalt-porphyrin were identified as coproporphyrin III in both cases.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 99 (1974), S. 181-201 
    ISSN: 1432-072X
    Keywords: Yeast ; Electronmicroscopy ; Microbody ; Peroxisome ; Catalase ; n-Alkane ; Utilizing Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Catalase activities of the cells growing onn-alkanes of various strains ofCandida yeasts wer markedly higher than those of the cells growing on glucose, ethanol or acetate. In connection with this, electron-microscopical studies revealed abundant appearance of specific microbodies having homogeneous matrix surrounded by single unit membrane in the hydrocarbon-growing cells. Localization of catalase activity in the microbodies, in addition to the mitochondria, was confirmed by cytochemical treatment of the cells with 3,3′-diaminobenzidine reagent.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; alkane utilization ; Yeast peroxisomes ; Long-chain alcohol dehydrogenase ; Long-chain aldehyde dehydrogenase ; Acyl-CoA synthetase ; Glycerol-3-phosphate acyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Long-chain alcohol dehydrogenase and longchain aldehyde dehydrogenase were induced in the cells of Candida tropicalis grown on n-alkanes. Subcellular localization of these dehydrogenases, together with that of acyl-CoA synthetase and glycerol-3-phosphate acyltransferase, was studied in terms of the metabolism of fatty acids derived from n-alkane substrates. Both longchain alcohol and aldehyde dehydrogenases distributed in the fractions of microsomes, mitochondria and peroxisomes obtained from the alkane-grown cells of C. tropicalis. Acyl-CoA synthetase was also located in these three fractions. Glycerol-3-phosphate acyltransferase was found in microsomes and mitochondria, in contrast to fatty acid β-oxidation system localized exclusively in peroxisomes. Similar results of the enzyme localization were also obtained with C. lipolytica grown on n-alkanes. These results suggest strongly that microsomal and mitochondrial dehydrogenases provide long-chain fatty acids to be utilized for lipid synthesis, whereas those in peroxisomes supply fatty acids to be degraded via β-oxidation to yield energy and cell constituents.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; Propionate ; Alkanes ; Acetate ; Carnitine acetyltransferase ; Catalase ; Propionate-activating enzyme ; Peroxisomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Candida tropicalis, a representative alkane- and higher fatty acid-utilizing yeast, can grow on propionate used as sole carbon and energy source. Initial pH of the medium markedly affected the growth of the yeast on propionate. In propionate-grown cells, several enzymes associated with peroxisomes and/or participating in propionate metabolism were induced in connection with the appearance of the characteristic peroxisomes. Acetate-grown cells of this yeast had only few peroxisomes, while alkane-grown cells contained conspicuous numbers of the organelles. As compared with alkane-grown cells, some specific features were observed in peroxisomes and enzymes associated with the organelles of propionate-grown cells: The shape of peroxisomes was large but the number was small; unlike localization of catalase in peroxisomes of alkane-grown cells, the enzyme of propionate-grown cells was mainly localized in cytoplasm; as for carnitine acetyltransferase localized almost equally in peroxisomes and mitochondria in alkane-grown cells, propionate-grown cells contained mainly the mitochondrial type enzyme. A propionate-activating enzyme, which was different from acetyl-CoA synthetase, was also induced in cytoplasm of propionate-grown cells. The role of carnitine acetyltransferase and the propionate-activating enzyme in propionate metabolism is discussed in comparison with the role of carnitine acetyltransferase and acetyl-CoA synthetase in acetate metabolism.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 112 (1977), S. 1-8 
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; Utilization of n-alkane ; Isolation of microbody ; Catalase ; Glyoxylate cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Microbodies appearing abundantly in n-alkane-grown cells of Candida tropicalis pK 233 were isolated by means of sucrose density gradient centrifugation. Electron microscopical observation showed that the microbodies isolated were intact. Localization of catalase and d-amino acid oxidase in the isolated microbodies was confirmed. Isocitrate lyase, malate synthase and NADP-linked isocitrate dehydrogenase were also located in the microbody, but malate dehydrogenase, citrate synthase, aconitase and NAD-linked isocitrate dehydrogenase were not. Neither cytochrome P-450 nor NADPH-cytochrome c reductase, the components involved in the n-alkane hydroxylation system of the yeast, were detected in the microbody fraction.
    Type of Medium: Electronic Resource
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