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Results 1 - 10 of 10
EC Number
Reaction
Commentary
Reference
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
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Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
A1-II with a glove-like beta-sandwich as a basic scaffold forms a cleft covered with two lid loops (L1/L2). Loop flexibility for substrate binding and structural determinants for broad substrate recognition and catalytic reaction is shown. The two loops associate mutually over the cleft through the formation of a hydrogen bond between their edges (Asn141 and Asn199)
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
alginate lyase activity and mannuronan C-5-epimerase activity of the bifunctional enzyme might use the same active site
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
also performs reaction of EC 4.2.2.11, the enzyme molecule shows a cleft which might bear the active site with a tryptophan residue being involved in the catalytic reaction
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
enzyme seems to have 6 substrate binding sites, also performs reaction of EC 4.2.2.11
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
His192 is an active site residue, essential for activity
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues, substrate binding mode, overview
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
substrate binding site structure, active site cleft, catalytic mechanism
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
substrate binding, strutural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
Results 1 - 10 of 10