Define \'transition state\' and the relationship between a transition state and

Question

Define 'transition state' and the relationship between a transition state and reaction rate. ii) Explain why mimics of enzymatic transition states are frequently potent inhibitors. Your answer should include an explanation why these mimics must be chemically stable. iii) Draw the mechanism of amide hydrolysis catalysed by a serine protease (e.g. chymotrypsin). Annotate the active site amino acid residues that are acting as general acid, base or nucleophilic catalysts. iv) List the properties of bortezomib that make it a good inhibitor of the chymotrypsin-like active site of the proteasome.

Explanation / Answer

Answer - i)

Transition State:

Definition: Transition state is a specific configuration of the molecule(s) formed through various chemical interactions like bond formation, bond breaking or some weak interactions loke hydrogen bonding.

This is the highest potential energy state of reactants in course of reaction and marked with sign double dagger ( ‡).

2) Relation between transition state and reaction rate :

i) Transition state theory states that,

a) Study of activated complexes lying near saddle point of potential energy can be used to study reaction rate. Saddle point itself is a T.S.

b) Activated complex is in quasi equilibrium state with reactatnt molecules.

c) Kinetic theory can be used to study reaction rate.

Transition State Theory find vast and useful application in enzymatic reactions.

===================XXXXXXXXXXXXXXXXXXX========================

Related Questions

Navigate

• Browse (All)
• Browse D
• Subjects

---

---

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.