Enzymatic activity can be regulated in several ways: allostery, covalent modific

Question

Enzymatic activity can be regulated in several ways: allostery, covalent modification, substrate cycling, regulation of gene transcription. Select two of these mechanisms and explain how they influence the activity of enzymes in general as well as how the enzymes for the flux-generating steps of glycolysis and fatty acid synthesis are regulated by one or more of these mechanisms?

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Explanation / Answer

1 allostery

The site the effector ties to is termed the allosteric site. Allosteric destinations permit effectors to tie to the protein, regularly bringing about a conformational change. Effectors that upgrade the protein's action are alluded to as allosteric activators, while those that abatement the protein's movement are called allosteric inhibitors.

Allosteric regulations are a characteristic case of control circles, for example, input from downstream items or feedforward from upstream substrates. Long-extend allostery is particularly essential in cell flagging Allosteric regulation is likewise especially critical in the cell's capacity to modify catalyst movement.

COVALENT MODIFICATION

The covalent connection of another atom can adjust the action of chemicals and numerous different proteins. In these occasions, a giver particle gives a useful moiety that alters the properties of the catalyst. Most adjustments are reversible. Phosphorylation and dephosphorylation are the most well-known however by all account not the only method for covalent change.

PART 2

GLYCOLYSIS - THE ENZYME INVOLVED IS Phosphofructokinase

ATP ACTS AS negative modulator AND BINDS AT REGULATORY SITE ( allostery)

FTTY ACID - Acetyl-CoA carboxylase is IS REGULATED BY both phosphorylation and allosteric regulation

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