Serine Proteases and Serine Protease Inhibitors

Abstract

Serine proteases are among the largest group of proteolytic enzymes in the human genome that play vital roles in health and disease. Regulation of their activity in vivo is mediated by a diverse group of serine protease inhibitors. An overview of the interplay between serine proteases and their inhibitors is provided. In addition, approaches to characterize this relationship are discussed with subsequent emphasis on how such measures apply to pathologies that result from defect of serine proteases or their inhibitors.

Jasmonate and ethylene dependent defence gene expression and suppression of fungal virulence factors: two essential mechanisms of Fusarium head blight resistance in wheat?

“…Dream transcriptome, serine PI proteins of the subtilisin-like protease (SLP) superfamily were significant enriched at both timepoints (Table 2), represented by the Go terms ‘serine-type endopeptidase inhibitor activity’ (GO:0004867) and ‘peptidase activity’ (GO:0008233). PI proteins generally feature a high substrate specificity and therefore, it is likely that those genes encode for proteins that specifically bind and impair secreted Fusarium SL proteases [97]. Proteases generally cause the proteolytic digestion of proteins via the hydrolysation of peptide bonds.…”

Risky circuitry? psychosocial risk factors and neural circuits in the development and persistence of eating disorders. A commentary on keel & forney and friederich et al.

“…Just as serine proteases are the most common class of protease in seminal fluid, serine protease inhibitors (including serpins and the Kazal‐ and Kunitz‐type inhibitors) are also the most prevalent class of protease inhibitors, though cysteine protease inhibitors are also common. The prevalence of serine proteases and their inhibitors in the seminal fluid is expected, given the large proportion of these classes in the proteome (Page et al, 2007): of 187 known or predicted protease inhibitors (and their homologues) in D. melanogaster , approximately 110 are inhibitors of serine proteases (Rawlings et al, 2012), of which 29 are serpins (Gubb et al, 2010). There are far more protease inhibitors in humans: 1,845 inhibitors and homologs in total, with at least 180 serine protease inhibitors (including 39 serpins), though it is not yet known which protease classes are inhibited by the majority of human predicted protease inhibitors (Rawlings et al, 2012).…”

A protease from Moringa oleifera Lam exhibits plasmin like activity of blood clot solubilization under ex-vivo and in-vitro hydrolysis of fibrin

“…Fibrinolytic enzymes have been classi ed into serine proteases, metalloproteases and serine metalloproteases types based on their catalytic mechanism [48]. Serine proteases have serine residue at active site that participates in catalysis [49]. Metalloproteases require metal ions (Zn 2+ or Co 2+ ) for catalysis [50].…”