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  • Beta  (2)
  • Glycollate metabolism  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 153 (1981), S. 225-231 
    ISSN: 1432-2048
    Keywords: Beta ; Glycollate decarboxylation ; Glyoxylate ; Hydroxypyruvate ; Leaf peroxisomes ; Serine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The linked utilization of glycollate and L-serine has been studied in peroxisomal preparations from leaves of spinach beet (Beta vulgaris L.). The generation of glycine from glycollate was found to be balanced by the production of hydroxypyruvate from serine and similarly by 2-oxoglutarate when L-glutamate was substituted for L-serine. In the presence of L-malate and catalytic quantities of NAD+, about 40% of the hydroxypyruvate was converted further to glycerate, whereas with substrate quantities of NADH, this conversion was almost quantitative. CO2 was released from the carboxyl groups of both glycollate and serine. Since the decarboxylation of both substrates was greatly in creased by the catalase inhibitor, 3-amino-1,2,4-triazole, and abolished by bovine liver catalase, it was attributed to the nonenzymic attack of H2O2, generated in glycollate oxidation, upon glyoxylate and hydroxypyruvate respectively. At 25–30° C, about 10% of the glyoxylate and hydroxypyruvate accumulated was decarboxylated, and the release of CO2 from each keto-acid was related to the amounts present. It is suggested that hydroxypyruvate decarboxylation might contribute significantly to photorespiration and provide a metabolic route for the complete oxidation of glycollate, the magnitude of this contribution depending upon the concentrations of glyoxylate and hydroxypyruvate in the peroxisomes.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Planta 153 (1981), S. 232-237 
    ISSN: 1432-2048
    Keywords: Beta ; Glutamate ; Glycollate metabolism ; Glyoxylate ; Glyoxylate aminotransferase ; Leaf peroxisomes ; Serine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When provided with glycollate, peroxisomal extracts of leaves of spinach beet (Beta vulgaris L. cv.) converted L-serine and L-glutamate to hydroxypyruvate and 2-oxoglutarate respectively. When approximately saturating concentrations of each of these amino acids were incubated separately with glycollate, the utilization of serine was greater than that of glutamate. The utilization of glutamate was substantially reduced by the presence of relatively low concentrations of serine in the reaction mixture, whereas even high concentrations of glutamate caused only small reductions in serine utilization. Over the entire range of concentrations of amino acids examined, serine was invariably the preferred amino-group donor, but this preference was abolished at higher concentrations of glyoxylate. Serine not only competed favourably for glyoxylate but also inhibited L-glutamate: glyoxylate aminotransferase (GGAT), the degree of inhibition depending upon the glyoxylate concentration. Studies of L-serine: glyoxylate aminotransferase (SGAT) and GGAT in partially purified extracts from spinach-beet leaves confirmed that serine competitively inhibited GGAT but glutamate did not affect SGAT. Both enzymes were inhibited by high glyoxylate concentrations, the inhibition being relieved by suitably high concentrations of the appropriate amino acid. It is concluded that at the low glyoxylate concentrations likely to occur in vivo, the preferential utilization of serine would ensure flux through the glycollate pathway to glycerate, but at higher concentrations of glyoxylate, both enzymes could be fully active in glyoxylate amination.
    Type of Medium: Electronic Resource
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