TY - JOUR
T1 - The mechanism of activation of heart fructose 6-phosphate,2-kinase:fructose-2,6-bisphosphatase
AU - Kitamura, K.
AU - Uyeda, K.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1987
Y1 - 1987
N2 - Partially purified fructose-6-P,2-kinase:fructose-2,6-bisphosphatase from beef heart was phosphorylated by cAMP protein kinase. The phosphorylated fructose-6-P,2-kinase shows lower K(m) for Fru-6-P (43 versus 105 μM) and for ATP (0.55 versus 1.3 mM) but no change in the V(max), compared to those for unphosphorylated enzyme. There was no detectable change in K(m) or V(max) of fructose-2,6-bisphosphatase activity by the phosphorylation. These changes in heart fructose-6-P,2-kinase were in direct contrast to previous results for the liver isozyme in which phosphorylation led to inhibition of the kinase activity and activation of the phosphatase activity.
AB - Partially purified fructose-6-P,2-kinase:fructose-2,6-bisphosphatase from beef heart was phosphorylated by cAMP protein kinase. The phosphorylated fructose-6-P,2-kinase shows lower K(m) for Fru-6-P (43 versus 105 μM) and for ATP (0.55 versus 1.3 mM) but no change in the V(max), compared to those for unphosphorylated enzyme. There was no detectable change in K(m) or V(max) of fructose-2,6-bisphosphatase activity by the phosphorylation. These changes in heart fructose-6-P,2-kinase were in direct contrast to previous results for the liver isozyme in which phosphorylation led to inhibition of the kinase activity and activation of the phosphatase activity.
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M3 - Article
C2 - 3027062
AN - SCOPUS:0023109218
SN - 0021-9258
VL - 262
SP - 679
EP - 681
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 2
ER -