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Inhibition of rat liver phosphofructokinase-2 by phosphoenolpyruvate and ADP.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kretschmer M,Hofmann E

doi

10.1016/0006-291x(84)91027-1

subject

Has Abstract

pub_date

1984-11-14 00:00:00

pages

793-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)91027-1

journal_volume

124

pub_type

杂志文章

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