Abstract
This chapter focuses on the properties of clostridial sialidases. These enzymes allow the bacteria to hydrolyze complex organic materials in their environment that originated from higher organisms such as animals. They use the liberated fatty, amino and nucleic acids, and carbohydrates for nutrition. The enzyme is thought to be of advantage to the bacteria, as it supplies them with a further source of energy that can be exploited if they produce N-acetylneuraminate lyase. The release of sialic acids makes sub-terminal structures accessible to digestion by other hydrolytic enzymes, whose products are made available to the bacteria. Sialidases are, therefore, believed to have a mainly nutritional function for these bacteria. Two bacterial sialidases are located in the cells that renders the enzymes inaccessible to their glycoconjugate substrates in the environment. The possible mechanisms of gene transfer are indicated by the finding that a flanking region of the Micromonospora viridifaciens sialidase gene exhibits homology with a transposon sequence.
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