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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 Pi for this reason).[1] A1AT is indeed the protease inhibitor most often involved in disease, namely in alpha 1-antitrypsin deficiency.
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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
References
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Wikipedia content modification information:
- This page was last modified on 11 October 2008, at 19:56.
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