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Polysaccharide lyases.

R J Linhardt, P M Galliher, C L Cooney

    Applied Biochemistry and Biotechnology
    |April 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Polysaccharide lyases are enzymes that degrade acidic polysaccharides via an eliminase mechanism, producing unsaturated oligosaccharides. This review covers microbial lyases acting on plant, animal, and microbial polysaccharides.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Carbohydrate Chemistry

    Background:

    • Polysaccharide lyases (EC 4.2.2.-), also known as eliminases, cleave activated glycosidic linkages in acidic polysaccharides.
    • These enzymes utilize an eliminase mechanism, distinct from hydrolysis, yielding unsaturated oligosaccharides.

    Purpose of the Study:

    • To review polysaccharide lyases acting on acidic polysaccharides from various origins (plant, animal, microbial).
    • To discuss the sources, regulation, purification, and properties of these enzymes, predominantly of microbial origin.

    Main Methods:

    • Literature review of polysaccharide lyases.
    • Compilation of information on enzyme classification (EC numbers), substrates, and mechanisms.
    • Summary of sources, regulation, purification, and properties.

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    Main Results:

    • Acidic polysaccharides and their degrading lyases are widespread.
    • Microbial sources, including pathogenic and nonpathogenic bacteria and fungi, are primary producers of these enzymes.
    • Specific lyases reviewed include alginate, pectin, pectate, chondroitin, hyaluronate, heparin, and heparan lyases.

    Conclusions:

    • Polysaccharide lyases are diverse enzymes crucial for degrading acidic polysaccharides.
    • Understanding their microbial origins, regulation, and properties is key to their applications.