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Helicobacter pylori enzymes.
Author(s) -
Nilius M,
Malfertheiner P
Publication year - 1996
Publication title -
alimentary pharmacology and therapeutics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.308
H-Index - 177
eISSN - 1365-2036
pISSN - 0269-2813
DOI - 10.1046/j.1365-2036.1996.22164007.x
Subject(s) - proteases , enzyme , helicobacter pylori , microbiology and biotechnology , catalase , mucus , biochemistry , biology , superoxide dismutase , urease , lactate dehydrogenase , acetaldehyde , phospholipase , atpase , proteolytic enzymes , ecology , genetics , ethanol
Helicobacter pylori exhibits a complex system of enzymes which serve a range of functions, such as colonization, damage of the host epithelium and provision of essential metabolic substrates. Colonization is favoured by urease and by the action on mucus and the mucosal barrier exerted by phospholipases and proteases, although this latter mechanism is controversial. Toxic effects are effected by urease, alcohol dehydrogenase (ADH), phospholipases and proteolytic enzymes. ADH produces acetaldehyde that is toxic to the mucosal cells, while phospholipases induce generation of products such as lysolecithin, which damage the gastric epithelium. Catalase and sodium dismutase of H. pylori are mainly involved in transforming toxic oxygen metabolites to harmless water; they protect the bacterium from the killing effect of neutrophils. Metabolic enzymes (for example, phosphatases, ATPases) are essential for the generation of energy, for synthesis and transport of cell products and for ion fluxes. In addition, they influence cell growth and the expression of virulence factors.