Phosphorylation of phosphofructokinase by protein kinase C changes the allosteric properties of the enzyme.

Abstract:

:The Ca2+- and phospholipid-dependent protein kinase C from rat brain phosphorylates rabbit muscle phosphofructokinase at the same trypsin-labile site as cyclic AMP-dependent protein kinase. However, protein kinase C also effectively phosphorylates one or more separate sites. Incubation of phosphofructokinase in the presence of protein kinase C, phospholipids, Ca2+, and ATP appears to affect the allosteric properties of phosphofructokinase by shifting the fructose 6-phosphate saturation curve to lower substrate concentrations in a time-dependent manner and decreasing cooperativity of the enzyme.

authors

Hofer HW,Schlatter S,Graefe M

doi

10.1016/0006-291x(85)91975-8

subject

Has Abstract

pub_date

1985-06-28 00:00:00

pages

892-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91975-8

journal_volume

129

pub_type

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