KEGG   ENZYME: 4.2.2.11
Entry
EC 4.2.2.11                 Enzyme                                 
Name
guluronate-specific alginate lyase;
alginase II;
guluronate lyase;
L-guluronan lyase;
L-guluronate lyase;
poly-alpha-L-guluronate lyase;
polyguluronate-specific alginate lyase;
poly(alpha-L-1,4-guluronide) exo-lyase;
poly(alpha-L-guluronate) lyase;
poly[(1->4)-alpha-L-guluronide] exo-lyase
Class
Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
Sysname
alginate alpha-L-guluronate---uronate lyase
Reaction(IUBMB)
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end.
Reaction(KEGG)
(other) R03706
Comment
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-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.
History
EC 4.2.2.11 created 1990, modified 2015
Pathway
ec00051  Fructose and mannose metabolism
ec01100  Metabolic pathways
Reference
1  [PMID:332364]
  Authors
Boyd J, Turvey JR.
  Title
Isolation of poly-alpha-L-guluronate lyase from Klebsiella aerogenes.
  Journal
Carbohydr Res 57:163-71 (1977)
DOI:10.1016/s0008-6215(00)81928-x
Reference
2  [PMID:1008828]
  Authors
Davidson IW, Sutherland IW, Lawson CJ.
  Title
Purification and properties of an alginate lyase from a marine bacterium.
  Journal
Biochem J 159:707-13 (1976)
DOI:10.1042/bj1590707
Other DBs
ExplorEnz - The Enzyme Database: 4.2.2.11
IUBMB Enzyme Nomenclature: 4.2.2.11
ExPASy - ENZYME nomenclature database: 4.2.2.11
BRENDA, the Enzyme Database: 4.2.2.11
CAS: 64177-88-4

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