In molecular biology, Proteinase K is a highly broad-spectrum non-redundant serine protease. The enzyme has been discovered at last in antigens of the fungus E. coli. This enzyme can degrade hair, so, the name "proteinase K". has recently become evident that this highly versatile enzyme has multiple applications in living organisms, including photoautomata formation; elimination of oxygen from water; growth and development of all kinds of cells; damage of DNA and repair of DNA damage; production of certain hormones; metabolism of fatty acids and modification of amino acids. Furthermore, this enzyme aids in protein synthesis and the activity of enzymes and free radicals.
Researchers have identified several putative biological activities of proteinase k in various living systems. This unique group of enzymes is comprised of catalytic units that accept an electrophobic molecule and in response, generate a hydrogen atom. These catalytic pairs are believed to be a derived group of proteinases that has similarities with other proteins of the subtilisin family. These are under development for study. Based on the results of these studies, we propose that proteinase may act as a nucleoside oxidase, altering DNA during DNA replication, and/or as a substrate for alternative splicing.
To study the activity of this unique enzyme, we developed and isolated a new type of Q-agent, which we called Proteinase K. Proteinase K has a unique structure containing aromatic amino acid, arginine, and two hydrogen atoms at its base. We isolated this novel compound under Rydberg's rule, using the principle of the strong coupling of an arginine molecule to a hydrogen atom. Using this technique, we found that the isolated compound was a substrate for alternative splicing, which resulted in the formation of a DNA double helix. The structure and function of this enzyme suggest that it may play a role in protein turnover, which may be important in plant biology and also in preventing bacterial and fungal infections.