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  • Electronic Resource  (3)
  • nuclear magnetic resonance  (3)
  • 1
    ISSN: 1573-4919
    Keywords: phosphomannoisomerase ; anomeric specificity ; nuclear magnetic resonance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The reversible conversion between D-mannose 6-phosphate and D-fructose 6-phosphate catalyzed by yeast phosphomannoisomerase was studied by phase sensitive 2D 13C-1H EXSY NMR spectroscopy at 100.623 MHz, using 13C enriched substrates in the C2 position of the D-hexose 6-phosphates. The unique pair of isomerization cross-peaks observed in the 2D EXSY map correlates the 13C2 resonances of the β-anomers of both D-[2-13C]-mannose-6-phosphate and D-[213C]-fructose 6-phosphate. This indicates that phosphomannoisomerase specifically catalyzes the reversible conversion between β-D-mannose 6-phosphate and β-D-fructose 6-phosphate. Since phosphoglucoisomerase was recently found to catalyze specifically the interconversion of α-D-glucose 6-phosphate and β-D-fructose 6-phosphate, the β-anomer of the ketohexose ester could be directly channeled in a multi-enzyme system involving phosphoglucoisomerase, phosphomannoisomerase and phosphofructokinase.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 103 (1991), S. 131-140 
    ISSN: 1573-4919
    Keywords: phosphoglucoisomerase ; nuclear magnetic resonance ; isotopic discrimination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The exchange of protons and deuterons by phosphoglucoisomerase during the single passage conversion of D-[2-13C,1-2H]fructose 6-phosphate in H2O or D-[2-13C]fructose 6-phosphate in D2O to D-[2-13C]glucose 6-phosphate, as coupled with the further generation of 6-phospho-D-[2-13C]gluconate in the presence of excess glucose-6-phosphate dehydrogenase was investigated by 13C NMR spectroscopy of the latter metabolite. In H2O, the intramolecular deuteron transfer from the C1 of D-fructose 6-phosphate to the C2 of D-glucose 6-phosphate amounted to 65%, a value only slightly lower than the 72% intramolecular proton transfer in D2O. Both percentages, especially the latter one, were lower than those previously recorded during the single passage conversion of D-[1-13C,2-2H]glucose 6-phosphate in H2O or D-[1-13C]glucose 6-phosphate in D2O to D-fructose 6-phosphate and then to D-fructose 1,6-bisphosphate. These differences indicate that the sequence of interactions between the hexose esters and the binding sites of phosphoglucoisomerase is not strictly in mirror image during, respectively, the conversion of the aldose phosphate to ketose phosphate and the opposite process.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4919
    Keywords: erythrocytes ; deuteration ; nuclear magnetic resonance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The production of C3-trisdeuterated, bisdeuterated, monodeuterated or non-deuterated L-[3-13C]lactate by human erythrocytes exposed to either D-[1-13C]glucose or D-[6-13C]glucose in the presence of2H2O can be assessed by13C NMR spectroscopy. Such a deuteration may occur at the level of the reactions catalyzed by phosphoglucoisomerase, phosphomannoisomerase, pyruvate kinase and glutamate-pyruvate transaminase. In this report, a mathematical model is proposed for the analysis of experimental data. It allows to estimate the relative extent of deuteration at each step of D-glucose metabolism. This approach may thus provide novel information on the extent of back-and-forth interconversion of either hexose 6-phosphates in both the phosphoglucoisomerase and phosphomannoisomerase reactions or pyruvate and L-alanine in the reaction catalyzed by glutamate-pyruvate transaminase.
    Type of Medium: Electronic Resource
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