4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	-	-	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	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)	693648	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	alginate lyase activity and mannuronan C-5-epimerase activity of the bifunctional enzyme might use the same active site	652156	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	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	-, 650644	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	beta-elimination mechanism, substrate binding and catalytic site	-, 648532	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	enzyme seems to have 6 substrate binding sites, also performs reaction of EC 4.2.2.11	-, 648533	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	His192 is an active site residue, essential for activity	652765	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	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	-, 729276	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	substrate binding site structure, active site cleft, catalytic mechanism	652853	
4.2.2.3	R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	substrate binding, strutural change and exolytic mechanism of alginate depolymerization by Alg17c, overview	-, 730063