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  • Pyrophosphate
  • Springer  (2)
  • MDPI Publishing
  • 1995-1999  (2)
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Keywords
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  • Springer  (2)
  • MDPI Publishing
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Purification and properties of the pyrophosphate-dependent phosphofructokinase from Dictyoglomus thermophilum Rt46 B.1 (1999)
    Springer
    Extremophiles 3 (1999), S. 131-137 
    Details
    ISSN: 1433-4909
    Keywords: Key words Phosphofructokinase ; Pyrophosphate ; Dictyoglomus thermophilum ; Polyphosphate ; Tripolyphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of phosphofructokinase phosphoryl donor subtypes (ATP-, ADP-, and pyrophosphate) in the deeply rooted phylogenetic lineages of thermophiles is of interest with regard to the evolution of phosphofructokinase activity and of the Embden–Meyerhof pathway. In this article we present the first biochemical description of a thermostable pyrophosphate-dependent phosphofructokinase from the hyperthermophilic bacterium Dictyoglomus thermophilum. The enzyme was not allosterically controlled by traditional modulators of phosphofructokinases and has significant activity with tripolyphosphate and polyphosphate. Kinetic parameters of the enzyme suggest it plays primarily a glycolytic role. The enzyme required Mg2+ for optimal activity, was partially activated by some monovalent and divalent cations, and was strongly inhibited by Cu2+. The sequence of the 21 N-terminal residues sug-gests that the enzyme is most similar to the pyrophosphate-dependent phosphofructokinases from Amycolatopsis methanolica and the hyperthermophilic crenarchaeon Thermoproteus tenax, enzymes which have been suggested to represent an ancient lineage of phosphofructoki-nases (Siebers et al. 1998). The unexpected finding of a pyrophosphate-dependent phosphofructokinase in Dictyoglomus thermophilum, which is phylogenetically related to Thermotoga maritima, previously shown to possess an ATP-dependent phosphofructokinase activity, is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050108
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  • 2
    Electronic Resource
    Electronic Resource
    Extraction of humic-β-glucosidase fractions from soil (1995)
    Springer
    Biology and fertility of soils 20 (1995), S. 77-82 
    Details
    ISSN: 1432-0789
    Keywords: Soil enzymes ; β-Glucosidase ; Humic/enzyme complexes ; Enzymatic extration ; Pyrophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Humic compounds with β-glucosidase activity were extracted from soil using tetrasodium pyrophosphate as extracting solution. Mixture of soil samples with 0.01 M pyrophosphate in a ratio of 1:5 (w/v), adjustment to pH 7.0–7.3, extraction for 18 h with reciprocating agitation, and bacteriological filtration after centrifugation were the optimum conditions for extraction of the β-glucosidase complexes. Otherwise, experimental conditions for extraction indicated that the concentration and pH of pyrophosphate were the factors with the most influence on enzymatic extraction yields. The results indicated that the β-glucosidase was extracellular and associated with soil humates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307845
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