Respuesta :
A Final statement or concluding statement PALA may activate ATCase at low Asp concentrations and saturating CP concentrations .
According to the Statement:
Instead of activation, inhibition occurs when PALA or Asp concentrations are high. The activation generated by low concentrations of PALA can be explained by the MWC model. The majority of the population of the enzyme does not transition to the R state at low Asp concentrations because the Asp concentration is insufficient to encourage this transition. As a result, the majority of the enzyme population is in the low-activity, low-affinity T state.
On the other hand, PALA binding, because of the way its structure resembles the transition state structure of the process, is able to keep the enzyme in the high-activity, high-affinity R state.
As a result, activity increases at low concentrations of PALA; but, as PALA concentration rises, more and more of the active sites are replaced by the non-hydrolyzable bisubstrate analog, and activity falls. At high Asp concentrations and a saturating CP concentration, PALA activation is not seen.
PALA binding just blocks the active site to which it binds and reduces activity because the enzyme population is already in the R state under these circumstances.
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A Final statement or concluding statement PALA may activate ATCase at low Asp concentrations and saturating CP concentrations .
However, increasing the concentration of PALA or Asp results in inhibition rather than activation. The MWC model can explain the activation caused by low amounts of PALA.
Because the Asp concentration is inadequate to promote the transition to the R state for the majority of the enzyme population at low Asp concentrations, the enzyme remains mostly in the low-activity, low-affinity T state. PALA binding, on the other hand, is able to maintain the enzyme in the high-activity, high-affinity R state because its structure mirrors the transition state structure of the process.
The concerted shift to the R state frees up the majority of active sites, allowing them to react with substrates and produce products, while a minority of active sites bound with PALA are inactive yet keep the enzyme in the R state.
As a result, activity rises at low PALA concentrations; but, as PALA concentration increases, more and more of the active sites are replaced by the non-hydrolyzable bisubstrate analog, and activity decreases. PALA activation is not detected at high Asp concentrations and a saturating concentration of CP.
Because the enzyme population is already in the R state under these conditions, PALA binding merely blocks the active site to which it binds and decreases activity.
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