Bestatin

Bestatin

Bestatin is a competitive inhibitor of aminopeptidase B, leucine aminopeptidase, and alanyl aminopeptidase. It is a small molecule derived from Streptomyces olivoreticuli, a species of bacteria in the genus Streptomyces. Bestatin is used in scientific research as a tool to probe the role of these enzymes in biological systems.

History

Bestatin was first isolated from Streptomyces olivoreticuli in the 1970s by Japanese researchers. It was initially identified for its antitumor properties, and has since been used in a variety of research contexts.

Mechanism of Action

Bestatin acts as a competitive inhibitor of several aminopeptidases, meaning it binds to the active site of these enzymes and prevents them from binding to their natural substrates. This inhibition can affect a variety of biological processes, as these enzymes are involved in the breakdown of proteins and peptides in the body.

Uses

Bestatin has been used in a variety of research contexts due to its ability to inhibit aminopeptidases. It has been used to study the role of these enzymes in cancer, inflammation, and immune response. In addition, it has been used in the development of new drugs and therapies.

Side Effects

As with any drug, Bestatin can have side effects. These can include nausea, vomiting, and diarrhea. However, these side effects are generally mild and temporary.

See Also

• Aminopeptidase
• Competitive inhibition
• Streptomyces

References

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