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- W314059907 abstract "Kinetic studies of L-Alanine dehydrogenase from Bacillus subtilis-catalyzed reactions in the presence of were carried out. The substrate (L-alanine) saturation curve is hyperbolic in the absence of the metal ion but it becomes sigmoidal when is added to the reaction mixture indicating the positive cooperative binding of the substrate in the presence of zinc ion. The cooperativity of substrate binding depends on the xinc ion concentration: the Hill coefficients () varied from 1.0 to 1.95 when the zinc ion concentration varied from 0 to . The inhibition of AlaDH by is reversible and noncompetitive with respect to (). itself binds to AlaDH with positive cooperativity and the cooperativity is independent of substrate concentration. The Hill coefficients of substrate biding in the presence of are not affected by the enzyme concentration indicating that binding does not change the polymerization-depolymerization equilibria of the enzyme. Among other metal ions, appears to be a specific reversible inhibitor inducing conformational change through the intersubunit interaction. These results indicate that is an allosteric competitive inhibitor and substrate being a non-cooperative per se, excludes the from its binding site and thus exhibits positive cooperativity. The allosteric mechanism of AlaDh from Bacillus subtilis is consistent with both MWC and Koshland's allosteric model." @default.
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- W314059907 date "1998-01-01" @default.
- W314059907 modified "2023-09-24" @default.
- W314059907 title "Unusual Allosteric Property of L-alanine Dehydrogenase from Bacillus subtilis" @default.
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