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Inhibition of ribose-5-phosphate isomerase by 4-phosphoerythronate.

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      Hoping to exploit the special affinity of enzymes for unstable intermediates in substrate transformation, we have determined the effectiveness of possible analogs of ene-diolate intermediates as inhibitors of spinach ribose-5-phosphate isomerase. 4-Phosphoerythronic acid was found to be a very strong competitive inhibitor, with a Ki value almost 3 orders of magnitude lower than the Km value of ribose 5-phosphate, and very much lower than the Ki value of any other inhibitor that was examined.

      REFERENCES

        • Horecker B.L.
        • Smymiotis P.Z.
        • Seegmiller J.E.
        J. Biol. Chem. 1951; 193: 383-396
        • Knowles F.C.
        • Pon N.G.
        J. Am. Chem. Soc. 1968; 90: 6536-6537
        • Fedtke C.
        Prog. Photosyn. Res. 1969; 3: 1597-1607
        • McDonough M.W.
        • Wood W.A.
        J. Biol. Chem. 1961; 236: 1220-1224
        • Noltmann E.A.
        Boyer P.D. The Enzymes. Academic Press, New York1972: 272-354
        • Rose I.A.
        Adv. Enzymol. Relat. Areas Mol. Biol. 1975; 43: 491-518
        • Wolfenden R.
        Annu. Rev. Biophys. 1976; 5: 271-306
        • Horecker B.L.
        Methods Enzymol. 1957; 3: 172-174
        • Klybas V.
        • Schramm M.
        • Racker E.
        Arch. Biochem. Biophys. 1959; 80: 229-237
        • Bandurski R.S.
        • Axelrod B.
        J. Biol. Chem. 1951; 193: 405-410
        • Knowles F.C.
        • Pon M.K.
        • Pon N.G.
        Anal. Biochem. 1969; 29: 40-47
        • Wilkinson G.N.
        Biochem. J. 1961; 80: 324-332
        • Axelrod B.
        • Jang R.
        J. Biol. Chem. 1954; 209: 847-855
        • Wolfenden R.
        Nature. 1969; 223: 704-705
        • Chirgwin J.M.
        • Noltmann E.A.
        Fed. Proc. 1973; 32: 667
        • Chirgwin J.M.
        • Noltmann E.A.
        J. Biol. Chem. 1975; 250: 7272-7276
        • Chirgwin J.M.
        • Parsons T.F.
        • Noltmann E.A.
        J. Biol. Chem. 1975; 250: 7277-7279