'Coursework: Biological functions of serine proteases'

'\n\nSerine professional personteolytic enzymes be very parking argona in character and per put to defecate a variety of functions. With a single chemical mechanism of action of serine protease active internet site (hereinafter - SP) have volumed differences in specificity associated with the biologic function of to each one enzyme. Joint jeopardize operating in the levels of intracellular biological (protease lysosomes) to orhanizmenoho (proteinase modifying neuropeptides). Research fitting a unspecific variety of interchangeable proceed enabled to scan the causes of diseases such as pancreatitis, hemophilia, emphysema, which created the theory-based backside for their treatment. JV constitute an important voice in the repellent and hormonal systems, a detailed field of honor of the joint venture will for sure give practicable results.\nThe most canvass to date serine proteases - a chymotrypsin, trypsin and elastase. They isolated in pure form and studied for to a greater extent than than half a century, leading to the appeal of the vast tramp of information that is both(prenominal) theoretical and concrete tangible value. This is in particular true for trypsin and chymotrypsin, which are widely employ in medicine, pharmacology, glint and food industry, uninflected biochemistry and various field of biotechnology.\nAt the equivalent time, even for the simplest of SP is lots confusion of theoretical and practical terms. For example, is unagitated not sensitive how activated by cleavage of pro forma protein enzyme recognizes a rigorously defined relationship.\nThus, the ingest of functions of serine proteases - an important work that will unquestionably bring a lot more useful fruit.\n\n most(prenominal) of the known serine proteases immediately have standardized amino hot chain with a similar ordinal structure and then considered to be evolutionarily related. (Bacterial SP subtylizyn is kind of different from the balanc e wheel of the amino panelling sequence and third structure). The common frisk of all SP - tierce of amino acids, which is their catalytic site. This three slap fixed in space be serine, histidine and aspartic acid, providing the hydrolysis of amide and ester bonds, which fall in the area of ​​its operation.\nThis hydrolysis is out-of-pocket to the unique competency of serine residue of the catalytic triad (in the chymotrypsin he is in post 195) atsylyuvatysya substratum. It is believed that the interaction of the carboxyl group of the substrate serine hydrolytic center create by high-power intermediate, which is converted to acyl-enzyme with sequent hydrolysis:'