Question

What is thought to be important in stabilizing the transition state of the bound substrates in the active site of aspartate transcarbamoylase?

Answer 1

The stabilization of the transition state in the active site of aspartate transcarbamoylase is important for proper enzyme function. Amino acid side chains can act as acid or base catalysts, and the folding of the polypeptide chain brings them close together in the active site. The induced fit model describes the dynamic interaction between enzyme and substrate.

Step-by-step explanation:

The stabilization of the transition state of bound substrates in the active site of aspartate transcarbamoylase is thought to be important for proper enzyme function. This is achieved through various mechanisms:

1. Amino acid side chains in or near the active site can act as acid or base catalysts, facilitating the necessary proton transfers during the reaction.
2. The folding and bending of the polypeptide chain brings the participating amino acids close together in the active site, allowing for efficient interaction between the enzyme and substrate.
3. The induced fit model suggests that the enzyme's structure undergoes a mild shift upon substrate binding, confirming an ideal binding arrangement between the enzyme and the transition state of the substrate.