| Literature DB >> 6239620 |
Abstract
Phosphofructokinase-2 from rat liver is inhibited by phosphoenolpyruvate and ADP. Phosphoenolpyruvate reduces the maximum activity in respect to fructose-6-phosphate and ATP but does not give rise to complete inhibition of phosphofructokinase-2. ADP increases the apparent Michaelis constant of the enzyme for ATP and leaves the maximum activity in respect to ATP unchanged. The apparent Michaelis constant for fructose-6-phosphate is not influenced by ADP.Entities:
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Year: 1984 PMID: 6239620 DOI: 10.1016/0006-291x(84)91027-1
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575