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PubMed:12970344 JSONTXT 21 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function

Id Subject Object Predicate Lexical cue
T1 0-54 Sentence denotes The three-dimensional structures of two beta-agarases.
T2 55-134 Sentence denotes Agars are important gelifying agents for biochemical use and the food industry.
T3 135-349 Sentence denotes To cleave the beta-1,4-linkages between beta-d-galactose and alpha-l-3,6-anhydro-galactose residues in the red algal galactans known as agars, marine bacteria produce polysaccharide hydrolases called beta-agarases.
T4 350-454 Sentence denotes Beta-agarases A and B from Zobellia galactanivorans Dsij have recently been biochemically characterized.
T5 455-525 Sentence denotes Here we report the first crystal structure of these two beta-agarases.
T6 526-700 Sentence denotes The two proteins were overproduced in Escherichia coli and crystallized, and the crystal structures were determined at 1.48 and 2.3 A for beta-agarases A and B, respectively.
T7 701-881 Sentence denotes The structure of beta-agarase A was solved by the multiple anomalous diffraction method, whereas beta-agarase B was solved with molecular replacement using beta-agarase A as model.
T8 882-1130 Sentence denotes Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic machinery, namely the nucleophilic residues Glu-147 and Glu-184 and the acid/base residues Glu-152 and Glu-189 for beta-agarases A and B, respectively.
T9 1131-1387 Sentence denotes The structures of the agarases were compared with those of two lichenases and of a kappa-carrageenase, which all belong to family 16 of the glycoside hydrolases in order to pinpoint the residues responsible for their widely differing substrate specificity.
T10 1388-1593 Sentence denotes The relationship between structure and enzymatic activity of the two beta-agarases from Z. galactanivorans Dsij was studied by analysis of the degradation products starting with different oligosaccharides.
T11 1594-1756 Sentence denotes The combination of the structural and biochemical results allowed the determination of the number of subsites present in the catalytic cleft of the beta-agarases.