The mechanism of activation of heart fructose 6-phosphate,2-kinase

fructose-2,6-bisphosphatase

K. Kitamura, K. Uyeda

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)679-681
Number of pages3
JournalJournal of Biological Chemistry
Volume262
Issue number2
StatePublished - 1987

Fingerprint

Phosphofructokinase-2
Chemical activation
Phosphorylation
Beef
Phosphoric Monoester Hydrolases
Liver
Protein Kinases
Isoenzymes
Phosphotransferases
Adenosine Triphosphate
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

The mechanism of activation of heart fructose 6-phosphate,2-kinase : fructose-2,6-bisphosphatase. / Kitamura, K.; Uyeda, K.

In: Journal of Biological Chemistry, Vol. 262, No. 2, 1987, p. 679-681.

Research output: Contribution to journalArticle

@article{2ffa3767138045a08ef1b6e7ddb48ae2,
title = "The mechanism of activation of heart fructose 6-phosphate,2-kinase: fructose-2,6-bisphosphatase",
abstract = "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.",
author = "K. Kitamura and K. Uyeda",
year = "1987",
language = "English (US)",
volume = "262",
pages = "679--681",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "2",

}

TY - JOUR

T1 - The mechanism of activation of heart fructose 6-phosphate,2-kinase

T2 - fructose-2,6-bisphosphatase

AU - Kitamura, K.

AU - Uyeda, K.

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.

UR - http://www.scopus.com/inward/record.url?scp=0023109218&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023109218&partnerID=8YFLogxK

M3 - Article

VL - 262

SP - 679

EP - 681

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 2

ER -