[HTML][HTML] Conversion of non-allosteric pyruvate kinase isozyme into an allosteric enzyme by a single amino acid substitution
Y Ikeda, T Tanaka, T Noguchi - Journal of Biological Chemistry, 1997 - ASBMB
Pyruvate kinase M 1, a non-allosteric isozyme, was converted into an allosteric enzyme by
replacement of an amino acid in the intersubunit contact. The substitution of Ala-398 with
Arg resulted in the pronounced allosteric enzyme. The Hill coefficient and the substrate
concentration giving one-half of V max for the mutant with respect to phosphoenolpyruvate
were 2.7 and 0.41 mm, respectively, whereas those values for the wild type were 1.0 and
0.049 mm. This mutation, however, gave rise to only minor effects on the apparent values of …
replacement of an amino acid in the intersubunit contact. The substitution of Ala-398 with
Arg resulted in the pronounced allosteric enzyme. The Hill coefficient and the substrate
concentration giving one-half of V max for the mutant with respect to phosphoenolpyruvate
were 2.7 and 0.41 mm, respectively, whereas those values for the wild type were 1.0 and
0.049 mm. This mutation, however, gave rise to only minor effects on the apparent values of …