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  • ATP:AMP phosphotransferase  (1)
  • C4-plant  (1)
  • Springer  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 27 (1995), S. 943-951 
    ISSN: 1573-5028
    Keywords: adenylate kinase ; ATP:AMP phosphotransferase ; rice ; expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Previously, we characterized nucleotide sequences of two cDNAs encoding adenylate kinase from rice plants (Oryza sativa L.). Each cDNA (Adk-a or Adk-b) was cloned into the expression vector pET 11d-GST to produce GST-AK fusion proteins in Escherichia coli. Recombinant proteins were cleaved by thrombin, and GST-free adenylate kinase proteins were obtained. Enzyme activity profiles of different pH and inhibition effects to the enzyme by Ap5A (adenosine-5′-pentaphospho-5′-adenosine) indicates that both adenylate kinase proteins have similar biochemical characteristics. Among the nucleoside monophosphates (AMP, CMP, GMP and UMP) investigated, only AMP reacted with ATP. Furthermore, using the antiserum against the rice adenylate kinase proteins, the cellular location of adenylate kinase proteins was examined by immunomicroscopic analysis in combination with a subcellular fractionation method. The results indicated that adenylate kinase proteins were distributed largely in cytosol of rice cells.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-9368
    Keywords: C4-plant ; maize ; phosphoenolpyruvate carboxylase ; quantum yield ; transgenic tobacco
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The expression of maize (Zea mays) phosphoenolpyruvate carboxylase (PEPC) gene constructs in transgenic tobacco plants (Nicotiana tabacum) was studied. Where transcription was under the control of a CaMV 35S promoter, maize PEPC transcripts of the correct size were detected. Western blot analysis indicated that the transgenic plants contained about twice as much PEPC as non-transformed plants. Furthermore, the enzymatic activity of PEPC in the leaves of these transgenic plants was up to twice as high as that in non-transformed plants. Two forms of PEPC with different kinetic properties were identified in leaf extracts of the transgenic plants: one form (the maize isoform) gave a high apparentK m value for phosphoenolpyruvate (PEP) and a high maximum activity, and the other (the tobacco isoform) exhibited a low apparentK m value for PEP and a low maximum activity. These biochemical differences resulted in several significant physiological changes in the transgenic plants: (1) the growth rate of the transgenic plants was lower than that of non-transgenic plants: (2) chlorophyll content per leaf area was relatively lower in the transgenic plants; and (3) the quantum yield of photosynthesis in the transgenic plants was not affected by changes in leaf temperature.
    Type of Medium: Electronic Resource
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