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Information on EC 4.2.2.11 - guluronate-specific alginate lyase

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.11 guluronate-specific alginate lyase
IUBMB Comments
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.
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UNIPROT: A9CEJ9
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
algmytc, guluronate-specific alginate lyase, guluronate lyase, alya1pl7, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alginase II
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guluronate lyase
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L-guluronan lyase
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L-guluronate lyase
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lyase, polyguluronate
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poly(1,4-alpha-L-guluronide)lyase
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poly(alpha-L-guluronate) lyase
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poly-alpha-L-guluronate lyase
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polyguluronate-specific alginate lyase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination of an alcohol from a polysaccharide
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
alginate alpha-L-guluronate-uronate lyase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
64177-88-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-L-guluronosyl linkage in alginate
?
show the reaction diagram
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.14
wild-type, pH 7.5, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
polysaccharide lyase family 15
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A9CEJ9_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
776
0
87871
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of native protein and its inactive mutant H531A in complex with alginate trisaccharide, at 2.10 and 2.99 A resolutions with final R-factors of 18.3 and 19.9%, respectively. The enzyme is comprised of an alpha/alpha-barrel plus anti-parallel beta-sheet as a basic scaffold. His311 and Tyr365 are the catalytic base and acid, respectively. A short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains are essential for the exolytic mode of action
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H311A
0.3% of wild-type activity
R199A
4.3% of wild-type activity
W467A
0.45% of wild-type activity
Y365F
0.011% of wild-type activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ochiai, A.; Yamasaki, M.; Mikami, B.; Hashimoto, W.; Murata, K.
Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens
J. Biol. Chem.
285
24519-24528
2010
Agrobacterium tumefaciens (A9CEJ9)
Manually annotated by BRENDA team