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Information on EC 4.2.2.3 - mannuronate-specific alginate lyase and Organism(s) Cobetia marina and UniProt Accession Q9ZNB7

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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:
Cobetia marina
UNIPROT: Q9ZNB7
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The taxonomic range for the selected organisms is: Cobetia marina
The enzyme appears in selected 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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-
-
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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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Poly(mana) alginate lyase
-
-
-
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poly(mana)alginate lyase
-
-
-
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SP2
-
-
-
-
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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-
-
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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
alginate
unsaturated algino-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
-
-
?
additional information
?
-
biological function of the enzyme
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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
unsaturated algino-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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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
assay methods, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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
LOCALIZATION PREDICTION?
ALGL_COBMA
374
0
42219
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 sp. (in: Bacteria), Bacillus sp. (in: Bacteria) ATB-1015, Chlorella virus (Q9QT64), Choromytilus meridionalis, Cobetia marina (Q9ZNB7), Colpomenia sinuosa, Corollospora intermedia, Dictyopteris pacifica, Dollabella auricola, Eisenia bicyclis, Endarachne binghamiae, Fucus spp., Haliotis corrugata, Haliotis tuberculata, Ishige sp., Laminaria digitata, Littorina sp., Niallia circulans, Paradendryphiella arenariae, Paradendryphiella salina, Pelvetia canaliculata, Perna perna, Photobacterium sp. (P39049), Pseudoalteromonas elyakovii (Q9Z6D6), Pseudomonas aeruginosa, Pseudomonas aeruginosa FRDI, Pseudomonas alginovora (Q59639), Pseudomonas alginovora XO17 (Q59639), Pseudomonas putida, Pseudomonas syringae, Sargassum sagamianum, Sphingomonas sp., Spisula solidissima, Stenotrophomonas maltophilia, Turbo cornutus, uncultured bacterium, uncultured bacterium Alg-A, Undaria pinnatifida, Vibrio alginolyticus, Vibrio sinaloensis, Vibrio sinaloensis Alg-A
Manually annotated by BRENDA team