Regular ArticleAntibody response of rabbits and cystic fibrosis patients to an alginate-specific outer membrane protein of a mucoid strain of Pseudomonas aeruginosa
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Alginate Lyase Aly36B is a New Bacterial Member of the Polysaccharide Lyase Family 36 and Catalyzes by a Novel Mechanism With Lysine as Both the Catalytic Base and Catalytic Acid
2019, Journal of Molecular BiologyCitation Excerpt :Some bacteria belonging to the Pseudomonas and Azotobacter genera also produce alginate. Bacterial alginates differ from those produced by brown algae in that they have little or no G-blocks and can be O-acetylated at some of the C-2 and C-3 carbons of the mannuronic acid residues [6–8]. Alginate lyases catalyze the degradation of alginate, targeting the glycosidic 1, 4 O-linkage via acid-base catalysis of β-elimination [9].
A complex multilevel attack on Pseudomonas aeruginosa algT/U expression and AlgT/U activity results in the loss of alginate production
2012, GeneCitation Excerpt :Alginate overproducing strains have outer membrane protein profiles with a prominent 54-kDa protein that is not observed in nonmucoid strains (Goldberg and Ohman, 1987; Grabert et al., 1990). The identity of the 54-kDa protein has been shown to be the product of the algE gene (Mathee et al., 1999), which is transcribed as part of an 18-kb operon of biosynthetic genes and appears to encode the porin component of a secretory complex involved in polymer export to the bacterial surface (Chu et al., 1991; Hay et al., 2010; Rehm et al., 1994a, 1994b). The mobility of the AlgE protein in SDS-PAGE is variable (Grabert et al., 1990).
Molecular characterization of Alg8, a putative glycosyltransferase, involved in alginate polymerisation
2009, Journal of Biotechnology