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Information on EC 4.2.2.3 - mannuronate-specific alginate lyase

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.3 mannuronate-specific alginate lyase
IUBMB Comments
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between beta-D-mannuronate 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 beta-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 4.2.2.11, guluronate-specific alginate lyase.
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UNIPROT: G9MBE4
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Word Map
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The enzyme appears in viruses and cellular organisms
Synonyms
alginate lyase, lysis protein, oligoalginate lyase, alg17c, a1-ii, aly-sj02, alg-5, a1-iii, hdaly, alypm, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alginate lyase
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alginate lyase I
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-
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alginate lyase VI
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AlgL
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lyase, alginate
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mannuronate alginate lyase
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-
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poly(1,4-beta-D-mannuronide) lyase
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-
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poly(beta-D-1,4-mannuronide) lyase
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-
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Poly(beta-D-mannuronate) lyase
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-
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Poly(mana) alginate lyase
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-
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poly(mana)alginate lyase
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-
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SP2
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
alginate beta-D-mannuronate-uronate lyase
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between beta-D-mannuronate 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 beta-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 4.2.2.11, guluronate-specific alginate lyase.
CAS REGISTRY NUMBER
COMMENTARY hide
86922-62-5
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9024-15-1
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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
poly(beta-D-mannuronate)
?
show the reaction diagram
the region including T121 of LbAly28 is the recognition of poly(MG) region of alginate
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the family PL-14
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G9MBE4_9CAEN
291
0
32277
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
x * 28000, recombinant His-tagged wild-type enzyme, SDS-PAGE, x * 28999, sequence calculation
28999
x * 28000, recombinant His-tagged wild-type enzyme, SDS-PAGE, x * 28999, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28000, recombinant His-tagged wild-type enzyme, SDS-PAGE, x * 28999, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K94A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
K97A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
R123A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
T121A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme, the replacement of T121 by Ala changes the substrate preference of LbAly28
Y135A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
Y137A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rahman, M.M.; Wang, L.; Inoue, A.; Ojima, T.
cDNA cloning and bacterial expression of a PL-14 alginate lyase from a herbivorous marine snail Littorina brevicula
Carbohydr. Res.
360
69-77
2012
Littorina brevicula (G9MBE4), Littorina brevicula
Manually annotated by BRENDA team