alpha 1-antitrypsin (A1AT, which is abbreviated PI for this reason).[3] 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 they inhibit, or by their mechanism of action. In 2004 Rawlings and colleagues introduced a classification of protease inhibitors based on similarities detectable at the level of amino acid sequence.
MEROPS database there are now 81 families of inhibitors. These families are named with an I followed by a number, for example, I14 contains hirudin
serpins. It contains inhibitors of multiple cysteine and serine protease families. Their mechanism of action relies on undergoing a large conformational change which inactivates their target's catalytic triad
Proteinase propeptide inhibitors (sometimes referred to as activation peptides) are responsible for the modulation of
beta-strands
with a (beta/alpha/beta)x2 topology.
The peptidase inhibitor I9 family contains the propeptide domain at the N-terminus of peptidases belonging to MEROPS family S8A, subtilisins. The propeptide is removed by proteolytic cleavage; removal activating the enzyme.
Inhibitor I10
Serine endopeptidase inhibitors
solution structure of marinostatin, a protease inhibitor, containing two ester linkages
proteolytic cleavage results in activation of the enzyme. This domain is also found, in one or more copies, in a variety of cysteine peptidase inhibitors such as salarin.[8]
Inhibitor I34
Saccharopepsin inhibitor I34
the structure of proteinase a complexed with an ia3 mutant inhibitor