The isotope-exchange reactions of ox heart phosphofructokinase

1. Ox heart phosphofructokinase catalyses isotope-exchange reactions at pH6.7 between ADP and ATP, and between fructose 6-phosphate and fructose 1,6-diphosphate, the latter reaction being absolutely dependent on the presence of the magnesium complex of ADP. 2. The reaction kinetics are hyperbolic wi...

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Bibliographic Details
Published inBiochemical journal Vol. 122; no. 2; pp. 181 - 187
Main Authors Hulme, E. C., Tipton, K. F.
Format Journal Article
LanguageEnglish
Published England 01.04.1971
Subjects
Adenine Nucleotides
Adenosine Triphosphate
Animals
Binding Sites
Carbon Isotopes
Cattle
Citrates
Fructosephosphates
Hydrogen-Ion Concentration
Kinetics
Magnesium
Molecular Weight
Myocardium - enzymology
Phosphofructokinase-1
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Summary:1. Ox heart phosphofructokinase catalyses isotope-exchange reactions at pH6.7 between ADP and ATP, and between fructose 6-phosphate and fructose 1,6-diphosphate, the latter reaction being absolutely dependent on the presence of the magnesium complex of ADP. 2. The reaction kinetics are hyperbolic with respect to substrate concentration for both exchange reactions (within the experimental error). 3. The influence of pH, AMP and citrate suggests that the fructose 6-phosphate–fructose 1,6-diphosphate exchange is subject to effector control, and is abolished by dissociation of the enzyme. 4. These results are discussed in relation to the reaction mechanism of the enzyme.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0306-3283
0264-6021
1470-8728
DOI:10.1042/bj1220181