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  • 11
    Electronic Resource
    Electronic Resource
    Induction and repression of arginase and ornithine transaminase in baker's yeast (1970)
    Springer
    Antonie van Leeuwenhoek 36 (1970), S. 1-19 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The arginase and the ornithine transaminase of baker's yeast are induced byl-arginine. Both enzymes have been shown to be repressed by nitrogen compounds. This is evidenced primarily by the decrease in specific enzyme activities caused by the addition of readily assimilable nitrogen compounds to a yeast culture with arginine, secondly by the derepression of both enzymes during nitrogen starvation of the yeast grown in various arginine-free media. This derepression equals both in rate and in amount the enzyme synthesis during the adaptation of the yeast to a medium withl-arginine as the sole nitrogen source. It is inhibited by various assimilable and non-assimilable amino acids. The derepression is the result of the nitrogen deficiency itself, since during the starvation of the yeast for sulphate, phosphate or magnesium, neither of the two enzymes is derepressed, and since it is independent of the nature of the carbon source in the nitrogen starvation medium, provided the latter is immediately assimilable. The enzymes are not subject to catabolite repression by glucose metabolites. It is concluded that the synthesis of arginase and ornithine transaminase in yeast is regulated by induction and repression. Arginine induces the enzymes; they are repressed by nitrogen compounds, probably in cooperation with one or more vitamins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02069003
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  • 12
    Electronic Resource
    Electronic Resource
    Nitrogen metabolite repression of arginase, ornithine transaminase and allantoinase in a conditional ethionine-resistant mutant of Saccharomyces cerevisiae with low activity of catabolic NAD-specific glutamate dehydrogenase (1982)
    Springer
    Antonie van Leeuwenhoek 48 (1982), S. 417-432 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00448414
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  • 13
    Electronic Resource
    Electronic Resource
    Growth of Candida famata and Trichosporon cutaneum on uric acid as the sole source of carbon and energy, a hitherto unknown property of yeasts (1983)
    Springer
    Antonie van Leeuwenhoek 49 (1983), S. 361-368 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Yeast strains capable of utilizing uric acid as the sole source of carbon and energy were isolated from soil by the enrichment culture method. The strains were identified as Candida famata (Harrison) Meyer et Yarrow and Trichosporon cutaneum (De Beurm., Gougerot et Vaucher) Ota. On the subcellular level growth of yeasts on uric acid was accompanied with the development of a number of large microbodies in the cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00399316
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  • 14
    Electronic Resource
    Electronic Resource
    Trichosporon adeninovorans sp. nov., a yeast species utilizing adenine, xanthine, uric acid, putrescine and primary n-alkylamines as the sole source of carbon, nitrogen and energy (1984)
    Springer
    Antonie van Leeuwenhoek 50 (1984), S. 369-378 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A new yeast species, Trichosporon adeninovorans, was isolated from soil by the enrichment culture method. Apart from adenine, the strain utilized uric acid, guanine, xanthine, hypoxanthine, 6,8-dihydroxypurine, putrescine, propylamine, butylamine, pentylamine, hexylamine and octylamine as sole source of carbon, nitrogen and energy. The structure of the cell wall of Tr. adeninovorans was ascomycetous. On the subcellular level growth on adenine or uric acid was accompanied with the development of microbodies in the cell. These cell organelles probably were the site of urate oxidase, an enzyme that, after growth on purine substrates, together with allantoinase was present at high activities. Low activities of adenine amidohydrolase and xanthine dehydrogenase were also demonstrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394651
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  • 15
    Electronic Resource
    Electronic Resource
    A mutant of Saccharomyces cerevisiae lacking catabolic NAD-specific glutamate dehydrogenase Growth characteristics of the mutant and regulation of enzyme synthesis in the wild-type strain (1978)
    Springer
    Antonie van Leeuwenhoek 44 (1978), S. 311-320 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract NAD-specific glutamate dehydrogenase (GDH-B)1 was induced in a wild-type strain derived of α-Σ 1278b by α-amino acids, the nitrogen of which according to known degradative pathways is transferred to 2-oxoglutarate. A recessive mutant (gdhB) devoid of GDH-B activity grew more slowly than the wild type if one of these amino acids was the sole source of nitrogen. Addition of ammonium chloride, glutamine, asparagine or serine to growth media with inducing α-amino acids as the main nitrogen source increased the growth rate of the gdhB mutant to the wild-type level and repressed GDH-B synthesis in the wild type. Arginine, urea and allantoin similarly increased the growth rate of the gdhB mutant and repressed GDH-B synthesis in the presence of glutamate, but not in the presence of aspartate, alanine or proline as the main nitrogen source. These observations are consistent with the view that GDH-B in vivo deaminates glutamate. Ammonium ions are required for the biosynthesis of glutamine, asparagine, arginine, histidine and purine and pyrimidine bases. Aspartate and alanine apparently are more potent inducers of GDH-B than glutamate. Anabolic NADP-specific glutamate dehydrogenase (GDH-A) can not fulfil the function of GDH-B in the gdhB mutant. This is concluded from the equal growth rates in glutamate, aspartate and proline media as observed with a gdhB mutant and with a gdhA, gdhB double mutant in which both glutamate dehydrogenases are lacking. The double mutant showed an anomalous growth behaviour, growth rates on several nitrogen sources being unexpectedly low.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394308
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  • 16
    Electronic Resource
    Electronic Resource
    Enzyme repression in the arginine pathway ofSaccharomyces cerevisiae (1969)
    Springer
    Antonie van Leeuwenhoek 35 (1969), S. 215-226 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Enzyme repression in the arginine pathway ofSaccharomyces cerevisiae was demonstrated by comparison of specific enzyme activities in yeast grown with and without arginine in various mineral salts media. Of the enzymes tested only ornithine transcarbamoylase was found to be repressed by exogenous arginine. Acetylornithine-glutamate transacetylase and argininosuccinate lyase were not affected. No relationship between specific enzyme activities and intracellular arginine concentration was observed. During the adaptation of yeast grown in a medium supplemented with amino acids to a mineral salts medium, the enzymes ornithine transcarbamoylase and argininosuccinate lyase were not derepressed beyond their specific activities normally present in yeast grown in mineral salts media. Neither were the arginine-degrading enzymes arginase and ornithine transaminase broken down during this adaptation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02219132
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  • 17
    Electronic Resource
    Electronic Resource
    Starch degradation by the mould Trichoderma viride I. The mechanism of starch degradation (1976)
    Springer
    Antonie van Leeuwenhoek 42 (1976), S. 229-238 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The mechanism of starch degradation by the fungus Trichoderma viride was studied in strain CBS 354.44, which utilizes glucose, starch and dextrins but is unable to assimilate maltose. It was shown that the amylolytic enzyme system is completely extracellular, equally well induced by starch, amylose or amylopectin and that it consists mainly of enzymes of the glucoamylase type which yield glucose as the main product of starch hydrolysis. Small amounts of α-amylase are produced also. The enzymes produced in starch cultures degrade starch, amylose and amylopectin equally well. Enzyme synthesis in starch media takes place to a considerable extent after exhaustion of the carbon source when maximum growth has been attained. Low-molecular dextrins are degraded by extracellular enzymes of the glucoamylase type. These enzymes are produced in media containing starch or dextrins. Maltotriose is consumed for only one third leaving maltose in the culture filtrate. Maltose is hardly attacked and hardly induces any amylolytic enzyme activity. No stable α-glucosidase appears to be produced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394119
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  • 18
    Electronic Resource
    Electronic Resource
    Starch degradation by the mould Trichoderma viride II. Regulation of enzyme synthesis (1976)
    Springer
    Antonie van Leeuwenhoek 42 (1976), S. 239-244 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The synthesis of amylolytic enzymes by the maltose not-utilizing Trichoderma viride strain CBS 354.44 requires the presence of starch or dextrins. Several readily utilizable carbon sources such as glucose and glutamic acid were shown to exert a strong catabolite repression which completely inhibited enzyme induction by starch or dextrins. Enzyme synthesis occurs in the exponential and in the stationary growth phase. In the latter, the ratio between saccharifying and dextrinizing enzyme activity is invariably high. In the exponential growth phase this ratio depends on the nature of the inducing substrate. Growth on starch results in an initially high production of dextrinizing activity, the saccharifying one becoming predominant in the course of exponential growth. The latter activity in dextrin DE 30 cultures is predominant from the very beginning. Thus, the amylolytic enzyme system of T. viride consists of at least two different enzymes, the synthesis of each being controlled specifically. The careful regulation of the synthesis of the dextrinizing enzyme is discussed with special reference to the production of non-utilizable maltose by the latter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394120
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  • 19
    Electronic Resource
    Electronic Resource
    The substrate constant for the ammonium ion of growing (1976)
    Springer
    Antonie van Leeuwenhoek 42 (1976), S. 293-297 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The relation between ammonium concentration and growth rate was studied in steady state continuous cultures of Saccharomyces cerevisiae in nitrogenlimited glucose ammonium medium. This relation could be described by the Monod equation. A maximum specific growth rate of 0.41 h-1 and a substrate constant for ammonium of 5–11 μM were calculated. Ammonium was determined by a modification of the phenol hypochlorite method. A discussion of the results in view of literature data on the substrate constants for other nutrients is given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394126
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  • 20
    Electronic Resource
    Electronic Resource
    Degradation of caffeine byPseudomonas putida C3024; the effect of oxygen concentration (1984)
    Springer
    Antonie van Leeuwenhoek 50 (1984), S. 298-300 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02342153
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