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  • Peroxisome  (2)
  • Leaf enzymes  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Localization of β-oxidation enzymes in peroxisomes isolated from nonfatty plant tissues (1983)
    Springer
    Planta 159 (1983), S. 238-246 
    Details
    ISSN: 1432-2048
    Keywords: Acyl-CoA oxidase ; β-Oxidation enzymes ; Compartmentation ; Microbody ; Peroxisome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peroxisomes from spinach leaves, mungbean hypocotyls, and potato tubers catalyze a palmitoyl-CoA-dependent, KCN-insensitive O2 uptake. In the course of this reaction O2 is reduced to H2O2 in a 1:1 stoichiometry and palmitoyl-CoA oxidized, in a 1:1 stoichiometry, to a product serving as substrate for enoyl-CoA hydratase. These findings demonstrate the existence of a peroxisomal acyl-CoA oxidase in these tissues. Enoyl-CoA hydratase (EC 4.2.1.17), 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), and thiolase (EC 2.3.1.9) are also associated with the peroxisomes from mung-bean hypocotyls and potato tubers (as well as with spinach leaf peroxisomes as recently reported; Gerhardt 1981, FEBS Lett. 126, 71). The low activities of these enzymes in mitochondrial fractions seem to be due to contaminating peroxisomes since the ratio of β-oxidation enzyme activities to catalase activity did not significantly differ between peroxisomal and mitochondrial fractions isolated on sucrose density gradients. The proof of localization of β-oxidation enzymes in peroxisomes without glyoxysomal function leads to the concept that fatty-acid oxidation is a consistent basic function of the peroxisome in cells of higher plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397531
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  • 2
    Electronic Resource
    Electronic Resource
    L-lactate dehydrogenase from leaves of Capsella bursa-pastoris (L.) Med. (1979)
    Springer
    Planta 146 (1979), S. 567-574 
    Details
    ISSN: 1432-2048
    Keywords: Capsella ; L-Lactate dehydrogenase ; Leaf enzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By ammonium sulfate fractionation and gel filtration an enzyme preparation which catalyzed NAD+-dependent L-lactate oxidation (10-4 kat kg-1 protein), as well as NADH-dependent pyruvate reduction (10-3 kat kg-1 protein), was obtained from leaves of Capsella bursa-pastoris. This lactate dehydrogenase activity was not due to an unspecific activity of either glycolate oxidase, glycolate dehydrogenase, hydroxypyruvate reductase, alcohol dehydrogenase, or a malate oxidizing enzyme. These enzymes could be separated from the protein displaying lactate dehydrogenase activity by gel filtration and electrophoresis and distinguished from it by their known properties. The enzyme under consideration does not oxidize D-lactate, and reduces pyruvate to L-lactate (the configuration of which was determined using highly specific animal L-lactate dehydrogenase). Based on these results the studied Capsella leaf enzyme is classified as L-lactate dehydrogenase (EC 1.1.1.27). It has a Km value of 0.25 mmol l-1 (pH 7.0, 0.3 mmol l-1 NADH) for pyruvate and of 13 mmol l-1 (pH 7.8, 3 mmol l-1 NAD+) for L-lactate. Lactate dehydrogenase activity was also detected in the leaves of several other plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388833
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  • 3
    Electronic Resource
    Electronic Resource
    Carnitine-acyltransferase activity of mitochondria from mung-bean hypocotyls (1988)
    Springer
    Planta 174 (1988), S. 90-93 
    Details
    ISSN: 1432-2048
    Keywords: Carnitine acyltransferase ; Mitochondrion ; Peroxisome ; Vigna
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Carnitine-acyltransferase activity assayed with acetyl-CoA, octanoyl-CoA, or palmitoyl-CoA is associated with the mitochondrial but not with the peroxisomes of mung-bean hypocotyls. Using mitochondria as an enzyme source, a half-maximal reaction rate is obtained with a palmitoyl-CoA concentration approximately twice that required with acetyl-CoA. In the presence of a saturating acetyl-CoA concentration the carnitine-acyltransferase activity is not enhanced by palmitoyl-CoA as additional substrate. However, palmitoylcarnitine is formed in addition to acetylcarnitine, and the formation of acetylcarnitine is competitively inhibited by palmitoyl-CoA. It is concluded that the mitochondria of mung-bean hypocotyls possess a carnitine acyltransferase of broad substrate specificity with respect to the chainlength of the acyl-CoA and that the demonstration of a carnitine-palmitoyltransferase activity in plant mitochondria does not indicate the presence of a specific carnitine long-chain acyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394878
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