The enzyme catalyses the degradation of alginate by a β-elimination reaction. It cleaves the (1→4) bond between β-D-mannuronate and either α-L-guluronate or β-D-mannuronate, generating oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to four residues, with preference for shorter products. cf. EC 220.127.116.11, guluronate-specific alginate lyase.
Davidson, I.W., Lawson, C.J. and Sutherland, I.W. An alginate lysate from Azotobacter vinelandii phage. J. Gen. Microbiol.98 (1977) 223–229. [DOI] [PMID: 13144]
Nakada, H.I. and Sweeny, P.C. Alginic acid degradation by eliminases from abalone hepatopancreas. J. Biol. Chem.242 (1967) 845–851. [PMID: 6020438]
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. [PMID: 14488584]
[EC 18.104.22.168 created 1965 as EC 22.214.171.124, transferred 1972 to EC 126.96.36.199, modified 1990, modified 2015]