Retroviruses affect a large number of species, from fish and birds to mammals and humans, with global socioeconomic negative impacts. Here the authors report and experimentally validate a novel approach for the analysis of the molecular networks that are involved in the recognition of substrates by retroviral proteases. Using multivariate analysis of the sequence-based physiochemical descriptio...

Proteases are found in all life forms. Initially proteases were described from gastric juices and thought to be involved in nonspecific degradation of proteins. While some proteases are nonspecific, others are highly specific both in their substrate selection and cleavage recognition sites. Proteases account for ~2% of the human genome with 553 defined members [1,2] and 1-5% of the genomes in i...

ATP-dependent proteases are found in nearly all living organisms and are known to play important roles in protein quality control, including protein degradation and protein refolding. ATP-dependent proteases have been well characterized in Escherichia coli. However, in the opportunistic human pathogen Pseudomonas aeruginosa, the role of these proteases is only starting to be understood. This re...

Porcine epidemic diarrhea coronavirus (PEDV) is currently devastating the United States pork industry by causing an 80-100% fatality rate in infected piglets. Coronavirus spike proteins mediate virus entry into cells, a process that requires the spike proteins to be proteolytically activated. It has been a conundrum which proteases activate PEDV entry. Here we systematically investigated the ro...

alkaline crude enzymes from the viscera of the tunisian barbel (barbus callensis) were extracted and characterized. proteolytic crude extract from barbel viscera was active and stable in alkaline solution. the optimum ph and temperature were 11.0 and 55 °c, respectively, using casein as a substrate. the crude alkaline protease was extremely stable in the ph range of 5.0-12.0. zymography activit...

Although protease-producing bacteria are key players in the degradation of organic nitrogen and essential for the nitrogen recycling in marine sediments, diversity of both these bacteria and their extracellular proteases is still largely unknown. This study investigated the diversity of the cultivable protease-producing bacteria and their extracellular proteases in the sediments of the eutrophi...

Serine proteases comprise nearly one-third of all known proteases identified to date and play crucial roles in a wide variety of cellular as well as extracellular functions, including the process of blood clotting, protein digestion, cell signaling, inflammation, and protein processing. Their hallmark is that they contain the so-called "classical" catalytic Ser/His/Asp triad. Although the class...

Residue 225 in serine proteases is typically Pro or Tyr and specifies an important and unanticipated functional aspect of this class of enzymes. Proteases with Y225, like thrombin, are involved in highly specialized functions like blood coagulation and complement that are exclusively found in vertebrates. In these proteases, the catalytic activity is enhanced allosterically by Na+ binding. Prot...

Two of the major rat mast cell proteases, rat mast cell protease 1 (RMCP-1) and RMCP-2, have for many years served as important phenotypic markers for studies of various aspects of mast cell (MC) biology. However, except for these proteases only fragmentary information has been available on the structure and complexity of proteases expressed by different subpopulations of rat MCs. To address th...