In biology and biochemistry, protease inhibitors are molecules that inhibit the function of peptidases (old name: protease, hence the term protease inhibitor). Many naturally occurring protease inhibitors are proteins.

In medicine, protease inhibitor is often used interchangeably with alpha 1-antitrypsin (A1AT, which is abbreviated P_i for this reason).^[1] A1AT is indeed the protease inhibitor most often involved in disease, namely in alpha 1-antitrypsin deficiency.

Classification

Protease inhibitors may be classified either by the type of protease the inhibit, or by their mechanism of action.

By protease

Classes of proteases are:

• Cysteine protease inhibitors
• Serine protease inhibitors (serpins)
  • Trypsin inhibitors
• Threonine protease inhibitors
• Aspartic protease inhibitors
• Metalloprotease inhibitors

By mechanism

Classes of inhibitor mechanisms of action are:

• Suicide inhibitor
• Transition state inhibitor
• Protein protease inhibitor (see serpins)
• Chelating agents

Compounds

• Aprotinin
• Bestatin
• Calpain inhibitor I and II
• Chymostatin
• E-64
• Leupeptin (N-acetyl-L-leucyl-L-leucyl-L-argininal)
• alpha-2-Macroglobuline
• Pefabloc SC
• Pepstatin
• PMSF (phenylmethanesulfonyl fluoride)
• TLCK
• Trypsin inhibitors

External links

• Sigma-Aldrich protease inhibitor overview

References

1. ^ OMIM - PROTEASE INHIBITOR 1; PI

This enzyme-related article is a stub. You can help Wikipedia by expanding it.