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Dual anomeric specificity of phosphomannoisomerase assessed by 2D phase sensitive 13C EXSY NMR

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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.

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Malaisse-Lagael, F., Willem, R., Penders, M. et al. Dual anomeric specificity of phosphomannoisomerase assessed by 2D phase sensitive 13C EXSY NMR. Mol Cell Biochem 115, 137–142 (1992). https://doi.org/10.1007/BF00230323

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