cAMP binding increases the Kd between the regulatory and catalytic subunits of PKA.Group of answer choicesTrueFalse
Question
cAMP binding increases the Kd between the regulatory and catalytic subunits of PKA.
Group of answer choices
- True
- False
Solution
The statement is False.
Explanation:
cAMP binding to Protein Kinase A (PKA) actually decreases the dissociation constant (Kd) between the regulatory and catalytic subunits. When cAMP binds to the regulatory subunits of PKA, it induces a conformational change that causes the regulatory subunits to release the catalytic subunits, thereby leading to an increase in kinase activity.
A lower Kd indicates a higher affinity, meaning the binding of cAMP reduces the strength of interaction between the regulatory and catalytic subunits. Thus, the presence of cAMP enhances the activation of PKA rather than increasing the Kd.
Similar Questions
The activity of phosphofructokinase 1 is increased by the binding ofGroup of answer choicesATPADPCitrateAcetyl CoATwo or more of the above
In Hatch & Slack pathway decarboxylation of C4 acid and regeneration of phosophoenol pyruvate occurs respectively in :-
Before entering the Krebs cycle, pyruvate is converted toMultiple ChoiceH2O and CO2.glucose.acetic acid.acetyl CoA.ATP.
The pentose phosphate pathway is regulated by __________*1 pointNone of these optionsAcetyl CoAAll optionsNADP+ATPNADPH
LDH and CYP enzymes are most likely to bind which substrates, respectively?A.NAPQI and APAPB.Lactate and APAPC.NAPQI and GSHD.Lactate and GSH
Upgrade your grade with Knowee
Get personalized homework help. Review tough concepts in more detail, or go deeper into your topic by exploring other relevant questions.