ИСТИНА

Soluble inorganic pyrophosphatases (PPases) are constitutive enzymes catalyzing the hydrolysis of inorganic pyrophosphate (PPi). This housekeeping reaction provides the driving force for numerous biosynthetic processes, including protein and DNA synthesis; this makes PPases absolutely indispensable enzymes for any living organism and, hence, attractive targets for the development of cytotoxic agents. Family I PPases include both eukaryotic and prokaryotic representatives. Their active site high conservation presents the major obstacle preventing targeting Family I PPases from pathogenic species for antimicrobial therapy. Some functional peculiarities of PPase from Mycobacterium tuberculosis (Mt-PPase) may be a basis for the development of its selective inhibitors. In this work, we made a systematic research on the characterization of the observed variability within Family I PPases using structural bioinformatics and computational approaches.