Are transition state analogs enzymes?

Transition state analog: A drug that binds to and therefore inhibits an enzyme because the drug resembles the transition state of a reaction normally catalyzed by the enzyme.

What makes a good transition state analog?

A good transition-state analog: binds covalently to the enzyme. binds to the enzyme more tightly than the substrate.

Why does the interaction of a transition state analogue with the enzyme take place?

Transition state analogs typically bind to enzyme active sites much more tightly than substrate analogs because the enzyme binds the substrate in the transition state more strongly than one in the ground state, as explained by the thermodynamic cycle as previously described.

Does transition state analog enhance enzyme activity?

Although the analog displays similar properties as the original transition molecule, but it has higher affinity for the enzyme than the natural substrate and will ultimately deactivate and inhibit the enzyme and prevent it from binding to a substrate.

What kind of inhibitors are transition state analogs?

Many are transition state analogs: Competitive inhibitors which mimic the transition state of an enzyme catalyzed reaction (e.g. HIV protease inhibitors such a Saquinavir and Viracept). Transition state analogs are compounds that resemble the transition state of a catalyzed reaction.

What is transition state enzyme?

The transitions state is the intermediary state of the reaction, when the molecule is neither a substrate or product. The transition state has the highest free energy, making it a rare and un-stable intermediate. An enzyme helps catalyze a reaction by decreasing the free energy of the transition state.

Which inhibitor is a transition state analog?

Examples of drugs that are transition state analog inhibitors include flu medications such as the neuraminidase inhibitor oseltamivir and the HIV protease inhibitors saquinavir in the treatment of AIDS.