Zeitschrift für Proteomik und Bioinformatik
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Abstrakt

Discoveries of Serine Protease Inhibitors from Scorpions

Md Abdul Hakim and Shilong Yang

 

Protease inhibitors (PIs) are proteins or peptides capable of inhibiting the catalytic activity of proteolytic enzymes. They are widely distributed in nature and can be found in all kingdoms of cellular life and also in viral genomes. It has previously been stated that a typical mammalian genome contains 2% – 4% of genes encoding for proteases or protease inhibitors, indicating the importance of proteolysis in their biological processes. However, many protease inhibitors have been reported to be present in animal venoms, suggesting that venomous animals use these proteins / peptides in their biological process of survival. Similarly, in recent years, some protease inhibitors have been reported to be present in scorpions and most of them have been identified by cDNA library screening or transcriptomic analysis. These protease inhibitors identified from scorpions have been described in two classes, such as 1) Kunitz-type inhibitors, and 2) Ascaris type inhibitors. Therefore, all the protease inhibitors identified to date from scorpions should be compiled based on their functional categories to help further understanding and research. Here, on the basis of published reports, this review describes about functions, primary sequences, structures, molecular mechanisms as well as functional diversity of the proteins/peptides from scorpions which have been reported to act as protease inhibitors. Summarily, here, we provide updated as well as amassed information about the scorpion protease inhibitors