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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Hofer HW,Schlatter S,Graefe Mdoi
10.1016/0006-291x(85)91975-8subject
Has Abstractpub_date
1985-06-28 00:00:00pages
892-7issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(85)91975-8journal_volume
129pub_type
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journal_title:Biochemical and biophysical research communications
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