Interaction of Candida Pyruvate Kinase with Cibacron Blue

概要

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Pyruvate kinase (ATP : pyruvate 2-O-phosphotransferase, EC 2.7.1.40) from several yeasts were adsorbed to blue dextran-Sepharose 4B and eluted with 1 M KCl in high yields. While pyruvate kinase of Candida guilliermondii AHU 4101 was eluted to some extent with phosphoenolpyruvate (PEP), ADP or fructose 1,6-diphosphate (FDP) individually from blue dextran-Sepharose 4B, the combination of FDP with PEP or ADP caused the complete elution of the kinase. Cibacron Blue competitively inhibited the pyuruvate kinase with respect to both PEP and ADP at a saturated level of fixed substrate in the presence of FDP, an allosteric activator. Further inhibition studies with Cibacron Blue suggest that one molecule of the blue dye binds per active site of the kinase at a saturated level of PEP, but two molecules of the dye bind per active site at an unsaturated level of PEP in the presence of FDP.
公益社団法人日本生物工学会の論文
1987-10-25