The Enzyme Database

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EC 4.2.2.11     
Accepted name: guluronate-specific alginate lyase
Reaction: Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and α-L-guluronate at their reducing end.
Other name(s): alginase II; guluronate lyase; L-guluronan lyase; L-guluronate lyase; poly-α-L-guluronate lyase; polyguluronate-specific alginate lyase; poly(α-L-1,4-guluronide) exo-lyase; poly(α-L-guluronate) lyase; poly[(1→4)-α-L-guluronide] exo-lyase
Systematic name: alginate α-L-guluronate—uronate lyase
Comments: The enzyme catalyses the degradation of alginate by a β-elimination reaction. It cleaves the (1→4) bond between α-L-guluronate 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 α-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64177-88-4
References:
1.  Boyd, J. and Turvey, J.R. Isolation of poly-α-L-guluronate lyase from Klebsiella aerogenes. Carbohydr. Res. 57 (1977) 163–171. [PMID: 332364]
2.  Davidson, I.W., Sutherland, I.W. and Lawson, C.J. Purification and properties of an alginate lyase from a marine bacterium. Biochem. J. 159 (1976) 707–713. [PMID: 1008828]
[EC 4.2.2.11 created 1990, modified 2015]
 
 


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