
Molecular-structural homology of proteolytic enzymеs in the studying of proteolysis mechanism and its regulation
Author(s) -
А. А. Чиркин,
О. М. Балаева-Тихомирова,
Viktoryia Dolmatova,
И. О. Семенов
Publication year - 2021
Publication title -
vescì nacyânalʹnaj akadèmìì navuk belarusì. seryâ hìmìčnyh navuk
Language(s) - English
Resource type - Journals
eISSN - 2524-2342
pISSN - 1561-8331
DOI - 10.29235/1561-8331-2021-57-2-206-217
Subject(s) - proteolysis , proteolytic enzymes , homology (biology) , biochemistry , enzyme , biology , computational biology , chemistry , amino acid
The actual problem of experimental medicine is the substantiation of new model organisms that meet modern requirements of bioethics, cost and conditions of detention. The aim of this work was a comparative analysis of the homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks. The homology of enzymes in nucleotide sequences in humans and pulmonary freshwater mollusks in the analysis of unregulated proteolysis is 66–68 %; regulated proteolysis – 69–76 %; ubiquitin-like modifiers – 78–83 %; extracellular enzymes – 67–76 %; and intracellular enzymes – 65–72 %. The evolutionary conservatism of proteolytic enzymes and the presence of an open blood circulation, which allows the substances under study to be delivered from the hemolymph directly to target cells, make it possible to use these animals as cheap and convenient test organisms. The practical importance of a sufficiently high homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks justifies the expediency of forming mollusk aquaculture to obtain proteolytic enzyme protein preparations from their tissues within the framework of the tasks of biopharmaceuticals, cosmetics and the food industry.