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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: Q9QT64
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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, a1-iii, alg-5, alge7, hdaly, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alginate lyase
-
Lysis protein
-
alginate lyase I
-
-
-
-
alginate lyase VI
-
-
-
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AlgL
-
-
-
-
lyase, alginate
-
-
-
-
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
-
-
-
-
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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-
-
-
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
-
9024-15-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alginate
?
show the reaction diagram
-
-
?
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
?
-
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
-
?
additional information
?
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biological function of the enzyme
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
required
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.021
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9QT64_9PHYC
333
0
36833
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 39000, recombinant enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli, 4.8fold
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cl2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli as His-tagged protein
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
Suda, K.; Tanji, Y.; Hori, K.; Unno, H.
Evidence for a novel Chlorella virus-encoded alginate lyase
FEMS Microbiol. Lett.
180
45-53
1999
Chlorella virus (Q9QT64), Chlorella virus
Manually annotated by BRENDA team