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  • 1
    Electronic Resource
    Electronic Resource
    Induction and subcellular localization of enzymes participating in propionate metabolism in Candida tropicalis (1983)
    Springer
    Archives of microbiology 136 (1983), S. 169-176 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00409839
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  • 2
    Electronic Resource
    Electronic Resource
    Purification of peroxisomal malate synthase from alkane-grown Candida tropicalis and some properties of the purified enzyme (1986)
    Springer
    Archives of microbiology 144 (1986), S. 137-141 
    Details
    ISSN: 1432-072X
    Keywords: Malate synthase ; Peroxisomes ; Alkane-grown yeast ; Candida tropicalis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Malate synthase, one of the key enzymes in the glyoxylate cycle, was purified from peroxisomes of alkane-grown yeast, Candida tropicalis. The enzyme was mainly localized in the matrix of peroxisomes, judging from subcellular fractionation followed by exposure of the organelles to hypotonic conditions. The molecular mass of this peroxisomal malate synthase was determined to be 250,000 daltons by gel filtration on a Sepharose 6B column as well as by ultracentrifugation. On sodium dodecylsulfate/polyacrylamide slab-gel electrophoresis, the molecular mass of the subunit of the enzyme was demonstrated to be 61,000 daltons. These results revealed that the native form of this enzyme was homo-tetrameric. Peroxisomal malate synthase showed the optimal activity pH at 8.0 and absolutely required Mg2+ for enzymatic activity. The K m values for Mg2+, acetyl-CoA and glyoxylate were 4.7 mM, 80 μM and 1.0 mM, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414723
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  • 3
    Electronic Resource
    Electronic Resource
    Novel NADP-linked isocitrate dehydrogenase present in peroxisomes of n-alkane-utilizing yeast, Candida tropicalis: comparison with mitochondrial NAD-linked isocitrate dehydrogenase (1995)
    Springer
    Archives of microbiology 163 (1995), S. 104-111 
    Details
    ISSN: 1432-072X
    Keywords: Peroxisomal NADP-linked isocitrate dehydrogenase ; NAD-linked isocitrate dehydrogenase ; Candida tropicalis ; Peroxisomes ; Mitochondria ; Cytosol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peroxisomal NADP-linked isocitrate dehydrogenase (Ps-NADP-IDH) was purified for the first time from Candida tropicalis cells grown on n-alkane as a carbon source, which was effective in proliferation of peroxisomes. The properties of Ps-NADP-IDH were compared with those of mitochondrial NAD-linked isocitrate dehydrogenase (Mt-NAD-IDH) purified from the cells grown on acetate, in which peroxisomes did not proliferate. Ps-NADP-IDH was a homodimer of identical subunits (45 kDa), while Mt-NAD-IDH was suggested to be a heterooctamer composed of two types of subunits with different molecular masses (41 and 38 kDa). Kinetic studies revealed that Ps-NADP-IDH gave Michaelis-Menten saturation curves against isocitrate and NADP concentrations, whereas Mt-NAD-IDH was an allosteric enzyme regulated by ATP, AMP, and citrate. Inhibition by 2-oxoglutarate, a precursor of glutamate, was observed only for Ps-NADP-IDH. Both enzymes were inhibited by concomitant addition of oxalacetate and glyoxylate. The function of Ps-NADP-IDH seems to be completely discriminated from that of Mt-NAD-IDH as reflected by their distinct subcellular localizations. Furthermore, the properties of Ps-NADP-IDH were also compared with those of other mitochondrial and cytosolic IDHs from sources reported previously.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00381783
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  • 4
    Electronic Resource
    Electronic Resource
    High level expression of isocitrate lyase gene of n-alkane-utilizing yeast Candida tropicalis in Sacchromyces cerevisiae (1991)
    Springer
    Archives of microbiology 156 (1991), S. 439-443 
    Details
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; Saccharomyces cerevisiae ; Peroxisomes ; Isocitrate lyase ; GAL7 promoter ; High level expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genomic DNA of peroxisomal isocitrate lyase (ICL) isolated from an n-alkane-assimilating yeast, Candida tropicalis, was truncated to utilize the original open reading frame under the control of the GAL7 promoter and was expressed in Saccharomyces cerevisiae. The recombinant ICL was synthesized as a functionally active enzyme with a specific activity similar to the enzyme purified from C. tropicalis, and was accounted for approximately 30% of the total extractable proteins in the yeast cells. This recombinant enzyme was easily purified to homogeneity. N-Terminal amino acid sequence, molecular masses of native form and subunit, amino acid composition, peptide maps, and kinetic parameters of the recombinant ICL were essentially the same as those of ICL purified from C. tropicalis. From these facts, S. cerevisiae was suggested to be an excellent microorganism to highly express the genes encoding peroxisomal proteins of C. tropicalis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245389
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  • 5
    Electronic Resource
    Electronic Resource
    The upstream region of the isocitrate lyase gene (UPR-ICL) of Candida tropicalis induces gene expression in both Saccharomyces cerevisiae and Escherichia coli by acetate via two distinct promoters (1995)
    Springer
    Archives of microbiology 163 (1995), S. 322-328 
    Details
    ISSN: 1432-072X
    Keywords: Isocitrate lyase ; n-Alkane-utilizable yeast ; Candida tropicalis ; Saccharomyces cerevisiae ; Promoters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The upstream region of the isocitrate lyase gene (UPR-ICL, 1530bp) of an n-alkane-utilizable yeast, Candida tropicalis, induced gene expression in another yeast, Saccharomyces cerevisiae, when the yeasts were grown on acetate. Surprisingly, UPR-ICL displayed the same regulatory function in the bacterium Escherichia coli when grown on acetate. We determined the interesting nucleotide sequence of UPR-ICL. The deletion analysis of UPR-ICL in both cells revealed the presence of two distinct promoters: one was localized at-394 to-379 and regulated gene expression in S. cerevisiae; the other was tocated near the initiation codon and regulated gene expression in E. coli. The two promoter sequences were similar, but not identical to regulatory elements that have been previously reported in S. cerevisiae and E. coli, respectively. Accordingly, the possibility of novel regulatory mechanisms could not be excluded. This is an interesting example of the presence of distinct cis-acting regulatory elements responsible for the induction of gene expression in one gene by acetate in both S. cerevisiae and E. coli. Preservation of such promoters through evolution is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404204
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  • 6
    Electronic Resource
    Electronic Resource
    The upstream region of the isocitrate lyase gene (UPR-ICL) of Candida tropicalis induces gene expression in both Saccharomyces cerevisiae and Escherichia coli by acetate via two distinct promoters (1995)
    Springer
    Archives of microbiology 163 (1995), S. 322-328 
    Details
    ISSN: 1432-072X
    Keywords: Key words Isocitrate lyase ; n-Alkane-utilizable yeast ; Candida tropicalis ; Saccharomyces cerevisiae ; Promoters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The upstream region of the isocitrate lyase gene (UPR-ICL, 1530bp) of an n-alkane-utilizable yeast, Candida tropicalis, induced gene expression in another yeast, Saccharomyces cerevisiae, when the yeasts were grown on acetate. Surprisingly, UPR-ICL displayed the same regulatory function in the bacterium Escherichia coli when grown on acetate. We determined the interesting nucleotide sequence of UPR-ICL. The deletion analysis of UPR-ICL in both cells revealed the presence of two distinct promoters: one was localized at –394 to –379 and regulated gene expression in S. cerevisiae; the other was located near the initiation codon and regulated gene expression in E. coli. The two promoter sequences were similar, but not identical to regulatory elements that have been previously reported in S. cerevisiae and E. coli, respectively. Accordingly, the possibility of novel regulatory mechanisms could not be excluded. This is an interesting example of the presence of distinct cis-acting regulatory elements responsible for the induction of gene expression in one gene by acetate in both S. cerevisiae and E. coli. Preservation of such promoters through evolution is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404204
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    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Novel NADP-linked isocitrate dehydrogenase present in peroxisomes of n-alkane-utilizing yeast, Candida tropicalis: comparison with mitochondrial NAD-linked isocitrate dehydrogenase (1995)
    Springer
    Archives of microbiology 163 (1995), S. 104-111 
    Details
    ISSN: 1432-072X
    Keywords: Key words Peroxisomal NADP-linked isocitrate ; dehydrogenase ; NAD-linked isocitrate dehydrogenase ; Candida tropicalis ; Peroxisomes ; Mitochondria ; Cytosol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peroxisomal NADP-linked isocitrate dehydrogenase (Ps-NADP-IDH) was purified for the first time from Candida tropicalis cells grown on n-alkane as a carbon source, which was effective in proliferation of peroxisomes. The properties of Ps-NADP-IDH were compared with those of mitochondrial NAD-linked isocitrate dehydrogenase (Mt-NAD-IDH) purified from the cells grown on acetate, in which peroxisomes did not proliferate. Ps-NADP-IDH was a homod imer of identical subunits (45 kDa), while Mt-NAD-IDH was suggested to be a heterooctamer composed of two types of subunits with different molecular masses (41 and 38 kDa). Kinetic studies revealed that Ps-NADP-IDH gave Michaelis-Menten saturation curves against isocitrate and NADP concentrations, whereas Mt-NAD-IDH was an allosteric enzyme regulated by ATP, AMP, and citrate. Inhibition by 2-oxoglutarate, a precursor of glutamate, was observed only for Ps-NADP-IDH. Both enzymes were inhibited by concomitant addition of oxalacetate and glyoxylate. The function of Ps-NADP-IDH seems to be completely discriminated from that of Mt-NAD-IDH as reflected by their distinct subcellular localizations. Furthermore, the properties of Ps-NADP-IDH were also compared with those of other mitochondrial and cytosolic IDHs from sources reported previously.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00381783
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    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Enhancement of carnitine acetyltransferase synthesis in alkane-grown cells and propionate-grown cells of Candida tropicalis (1985)
    Springer
    Archives of microbiology 141 (1985), S. 29-31 
    Details
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; n-Alkanes ; Propionate ; Carnitine acethyltransferase ; Peroxisomes ; Enzyme induction ; Immunochemical studies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The level of carnitine acetyltransferase was markedly increased in harmony with appearance of peroxisomes in alkane-grown cells and propionate-grown cells of Candida tropicalis. From immunochemical studies with antibodies against peroxisomal and mitochondrial carnitine acetyltransferases, it was confirmed that no other type of the enzyme than the peroxisomal and mitochondrial ones was present in alkane-, propionate- and glucose-grown cells of the yeast. The increase in the enzyme level in alkane- and propionate-grown cells was immunochemically proved to result from the increase in the amount of the enzyme protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446735
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    Paper (German National Licenses)
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