Immucillin H

Immucillin H

Immucillin H is a powerful transition state analogue inhibitor of purine nucleoside phosphorylase (PNP), an enzyme involved in the purine metabolism pathway. It was developed by Vern Schramm and colleagues at Albert Einstein College of Medicine.

Structure and Mechanism

Immucillin H is a synthetic analogue of the transition state of the reaction catalyzed by PNP. It is structurally similar to the natural substrate of PNP, inosine, but with modifications that allow it to bind to the enzyme more tightly. The key feature of Immucillin H is a cyclopentane ring, which mimics the ribose ring of inosine in its half-chair conformation, the shape it adopts during the transition state of the PNP-catalyzed reaction.

Therapeutic Use

Due to its potent inhibition of PNP, Immucillin H has potential therapeutic applications in the treatment of disorders related to purine metabolism, such as gout, hyperuricemia, and certain immune disorders. It has also been investigated for use in the treatment of malaria, as the Plasmodium parasite that causes malaria relies on PNP for survival.

Research and Development

The development of Immucillin H was a significant achievement in the field of enzyme inhibition and drug design. It demonstrated the potential of transition state analogue inhibitors as therapeutic agents, and paved the way for the development of other drugs based on the same principle.

See Also

• Transition state
• Enzyme inhibitor
• Drug design