Abstract：
:We have proposed an allosteric ATP inhibition mechanism of Pfk-2 determining the structure of different forms of the enzyme together with a kinetic enzyme analysis. Here we complement the mechanism by using hybrid oligomers of the homodimeric enzyme to get insights about the allosteric communication pathways between the same sites or different ones located in different subunits. Kinetic analysis of the hybrid enzymes indicate that homotropic interactions between allosteric sites for ATP or between substrate sites for fructose-6-P have a minor effect on the enzymatic inhibition induced by ATP. In fact, the sigmoid response for fructose-6-P observed at elevated ATP concentrations can be eliminated even though the enzymatic inhibition is still operative. Nevertheless, leverage coupling analysis supports heterotropic interactions between the allosteric ATP and fructose-6-P binding occurring between and within each subunit.
journal_name
Biochimiejournal_title
Biochimieauthors
Villalobos P,Soto F,Baez M,Babul Jdoi
10.1016/j.biochi.2016.08.013subject
Has Abstractpub_date
2016-09-01 00:00:00pages
209-16eissn
0300-9084issn
1638-6183pii
S0300-9084(16)30166-3journal_volume
128-129pub_type
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