Reaction: Eliminative cleavage of polysaccharides containing β-D-mannuronate residues to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends
Other name(s): alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly(β-D-1,4-mannuronide) lyase; aly (gene name)
Systematic name: poly[(1→4)-β-D-mannuronide] lyase
Comments: The enzyme from the bacterium Sphingomonas sp. strain A1 cleaves alginate producing di- and trisaccharides with an unsaturated uronyl residue at the non-reducing terminus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-15-1
1. Davidson, I.W., Lawson, C.J. and Sutherland, I.W. An alginate lysate from Azotobacter vinelandii phage. J. Gen. Microbiol. 98 (1977) 223-229. [PMID: 13144]
2. Nakada, H.I. and Sweeny, P.C. Alginic acid degradation by eliminases from abalone hepatopancreas. J. Biol. Chem. 242 (1967) 845-851. [PMID: 6020438]
3. Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid. J. Biol. Chem. 237 (1962) 309-316.
4. Hashimoto, W., Miyake, O., Momma, K., Kawai, S. and Murata, K. Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. J. Bacteriol. 182 (2000) 4572-4577. [PMID: 10913091]