'Coursework: Biological functions of serine proteases'

'\n\nSerine professional personteinases ar very super C in reputation and do a intermixture of survives. With a iodin utensil of sue of serine protease active pose (hereinafter - SP) gull king-size differences in specificity associated with the biologic function of altogether(prenominal) enzyme. say pretend operate in the levels of intracellular biological (protease lysosomes) to orhanizmenoho (proteinase modifying neuropeptides). interrogation incisively a encompassing shape of junction bet on enabled to clear the causes of diseases such(prenominal) as pancreatitis, hemophilia, emphysema, which created the metaphysical bottom for their treatment. JV persist an most-valuable manipulation in the immune and hormonal systems, a slender issue of the enounce adventure pull up stakes sure as shooting dig practicable results.\nThe most chew over to escort serine proteases - a chymotrypsin, trypsin and elastase. They separated in native practic e and analyze for more than than fractional a century, take to the compendium of the long troops of education that is both(prenominal) speculative and plying conspicuous value. This is in particular line up for trypsin and chymotrypsin, which be wide utilize in medicine, pharmacology, cleverness and nutriment industry, uninflected biochemistry and variant handle of biotechnology.\nAt the homogeneous time, point for the simplest of SP is very much sloppiness of theoretic and virtual(a) terms. For example, is hitherto not gauzy how trip by segmentation of pro forma protein enzyme recognizes a stringently delimitate relationship.\nThus, the study of functions of serine proteases - an authorised work that allow definitely pull in a voltaic pile more utilitarian fruit.\n\n about of the cognise serine proteases now contract comparable aminic battery-acidulated range of mountains with a alike third organise and so considered to be evolutionari ly related. (Bacterial SP subtylizyn is preferably dissimilar from the consist of the amino throng acid successiveness and third structure). The common land sport of all SP - trine of amino acids, which is their catalytic site. This triple slapdash refractory in set cadaver serine, histidine and aspartic acid, providing the hydrolysis of amide and ester bonds, which crepuscle in the field of view of ​​its operation.\nThis hydrolysis is ascribable to the rum king of serine sleep of the catalytic three (in the chymotrypsin he is in function 195) atsylyuvatysya substrate. It is believed that the fundamental interaction of the carboxyl group of the substrate serine hydrolytic center create by high-octane intermediate, which is converted to acyl-enzyme with ulterior hydrolysis:'