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- W2227384175 abstract "Enzymes that degrade poly-γ-glutamate (γ-PGA) are found mainly in bacteria. γ-PGA is a polymer of glutamic acid linked by γ-peptide bond synthesized by a membrane protein complex. It surrounds bacterial cells, and functions as a physical barrier against bacteriophages or phagocytosis and as an extracellular nutrient reservoir. γ-PGA-degrading enzymes of Bacillus subtilis, B. anthracis, Flavobacterium polyglutamicum, Myrothecium sp., and bacteriophages act differently on γ-PGA and they are essential to facilitate or to antagonize such physiological functions of γ-PGA. γ-PGA contains D-isomer of glutamic acid. γ-PGA-degrading enzymes recognize not only the γ-peptide bond but also the stereochemistry of the polymer. Among the γ-PGA-degrading enzymes, B. anthracis CapD and bacteriophage PghP have been examined in their tertiary structure. Catalytic mechanism and the recognition of stereochemistry of the substrate are discussed based on their 3D structures. Other γ-PGA-degrading enzymes are classified based on the mode of action and substrate specificities. Their catalytic and physiological functions are reviewed." @default.
- W2227384175 created "2016-06-24" @default.
- W2227384175 creator A5055016555 @default.
- W2227384175 creator A5063953413 @default.
- W2227384175 date "2010-01-01" @default.
- W2227384175 modified "2023-10-11" @default.
- W2227384175 title "Enzymatic Degradation of Poly-Gamma-Glutamic Acid" @default.
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- W2227384175 doi "https://doi.org/10.1007/978-3-642-12453-2_6" @default.
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