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Information on EC 4.2.2.3 - mannuronate-specific alginate lyase and Organism(s) Pseudomonas alginovora and UniProt Accession Q59639

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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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This record set is specific for:
Pseudomonas alginovora
UNIPROT: Q59639
Word Map
The taxonomic range for the selected organisms is: Pseudomonas alginovora
The enzyme appears in selected viruses and cellular organisms
Synonyms
(poly alpha-l-guluronate) lyase, A1 alginate lyase, A1-II, A1-III, A1-IV', A1m, A1mU, A9mC, A9mL, A9mT, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alginate lyase
alginate lyase I
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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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poly(1,4-beta-D-mannuronide) lyase
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poly(beta-D-1,4-mannuronide) lyase
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Poly(beta-D-mannuronate) lyase
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Poly(mana) alginate lyase
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poly(mana)alginate lyase
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SP2
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY SOURCE
PATHWAYS
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
alginate
oligosaccharides
show the reaction diagram
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
show the reaction diagram
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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
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
additional information
?
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biological function of the enzyme
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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required
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
assay methods, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
constitutive enzyme expression, recombinant enzyme
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ALYA_PSEAL
233
0
25873
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strains BL21(DE3), C41(DE3) and C43(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wong, T.Y.; Preston, L.A.; Schiller, N.L.
Alginate lyase: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
Annu. Rev. Microbiol.
54
289-340
2000
Alginovibrio aquatilis, Aplysia depilans, Asteromyces cruciatus, Azotobacter chroococcum, Azotobacter chroococcum (O50660), Azotobacter chroococcum 4A1M, Azotobacter phage A22, Azotobacter phage A31, Azotobacter vinelandii (O52195), Azotobacter vinelandii (Q9ZFG9), Azotobacter vinelandii phage, Bacillus circulans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) ATB-1015, Chlorella virus (Q9QT64), Choromytilus meridionalis, Cobetia marina (Q9ZNB7), Colpomenia sinuosa, Corollospora intermedia, Dollabella auricola, Eisenia bicyclis, Endarachne binghamiae, Fucus spp., Haliotis corrugata, Haliotis tuberculata, Ishige sp., Laminaria digitata, Littorina sp., Paradendryphiella arenariae, Paradendryphiella salina, Pelvetia canaliculata, Perna perna, Photobacterium sp. (P39049), Photobacterium sp. ATCC 43367, Photobacterium sp. ATCC 43367 Alg-A, Pseudoalteromonas sp. IAM14594 (Q9Z6D6), Pseudomonas aeruginosa, Pseudomonas aeruginosa FRDI, Pseudomonas alginovora (Q59639), Pseudomonas alginovora XO17 (Q59639), Pseudomonas putida, Pseudomonas syringae, Sargassum sagamianum, Spatoglossum pacificum, Sphingomonas sp., Spisula solidissima, Stenotrophomonas maltophilia, Turbo cornutus, uncultured bacterium, uncultured bacterium Alg-A, Undaria pinnatifida, Vibrio alginolyticus
Manually annotated by BRENDA team
Lundqvist, L.C.; Jam, M.; Barbeyron, T.; Czjzek, M.; Sandstroem, C.
Substrate specificity of the recombinant alginate lyase from the marine bacteria Pseudomonas alginovora
Carbohydr. Res.
352
44-50
2012
Pseudomonas alginovora, Pseudomonas alginovora X017
Manually annotated by BRENDA team
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