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Information on EC 4.2.2.3 - mannuronate-specific alginate lyase and Organism(s) Azotobacter vinelandii and UniProt Accession Q9ZFG9
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4.2.2.3 mannuronate-specific alginate lyaseIUBMB 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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Word Map
- 4.2.2.3
- polysaccharide
- lyases
- oligosaccharide
-
depolymerization
- polyg
- biotechnology
- seaweed
- colicins
- mucoid
- trisaccharide
-
uronic
- sphingomonas
-
alginate-degrading
-
exolytic
- pseudoalteromonas
- tetrasaccharide
-
beta-elimination
-
macroalgae
-
saccharification
- laminaria
-
holins
-
mannuronan
- saccharophagus
-
exo-type
- phix174
- sargassum
- medicine
- degradans
- murein
- microbulbifer
-
alginate-based
- endolysins
- abalone
- haliotis
-
polysaccharide-degrading
- analysis
- agriculture
- degradation
- molecular biology
- biofuel production
- food industry
- synthesis
The taxonomic range for the selected organisms is: Azotobacter vinelandii
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
alginate lyase, lysis protein, oligoalginate lyase, alg17c, a1-ii, aly-sj02, alg-5, a1-iii, hdaly, alypm, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alginate lyase
alginate lyase I
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-
-
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alginate lyase VI
-
-
-
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AlgL
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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-
-
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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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-
-
-
additional information
-
enzyme belongs to the family of secreted Ca2+-dependent epimerases
AlgL
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
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.
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.
alginate lyase activity and mannuronan C-5-epimerase activity of the bifunctional enzyme might use the same active site
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.
beta-elimination mechanism, substrate binding and catalytic site
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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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
86922-62-5
-
9024-15-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alginate
oligouronides
isoform AlgE7 degrades M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved are mainly G-MM and/or G-GM. G-moieties dominate at the reducing ends even when mannuronan is used as substrate, so the AlgE7 lyase/epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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-
?
alginate
oligosaccharides of 4-7 monomers
substrate from brown algae Macrocystis pyrifera rich in polymannuronate and polyguluronate, cleavage sequences are G-/-MM and/or G-/-GM
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?
G-alginate
?
-
purified alpha-L-guluronic acid blocks containing more than 90% alpha-L-guluronic acid
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-
?
MG-alginate
?
-
alginate epimerized by AlgE4 and containing 47% alpha-L-guluronic acid with no alpha-L-guluronic acid blocks, 100% activity
isoforms AlyA1, AlyA2, and AlyA3 produce mainly DELTAG and DELTAGMG as their end products, isoform AlyA3 produces as many trimers as it does dimers and tetramers
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
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-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
alginate
?
-
a heteropolysaccharides of alpha-L-guluronate and beta-D-mannuronate
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?
alginate
?
-
the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production
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?
alginate
oligouronides
alginate rich in mannuronic acids, the enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid bonds and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-beta-D-mannuronic acid bonds and alpha-L-guluronic acid-alpha-L-guluronic acid-bonds
-
-
?
alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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?
alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-alpha-L-guluronic acid or alpha-L-guluronic acid-beta-D-mannuronic acid bonds
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-
?
alginate
unsaturated algino-oligosaccharides
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isoforms AlyA1, AlyA2, and AlyA3 preferably cleave the bond between guluronic acid and mannuronic acid, resulting in a guluronic acid residue at the new reducing end, but isoform AlyA3 also degrades the other three possible bonds in alginate
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-
?
additional information
?
-
biological function of the enzyme
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?
additional information
?
-
biological function of the enzyme
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?
additional information
?
-
assay methods, overview, cleaves M-M and M-G linkages, but not G-GM linkages
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?
additional information
?
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assay methods, overview, cleaves M-M and M-G linkages, but not G-GM linkages
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?
additional information
?
-
cleaves G-MM and G-GM linkages, but nt G-GM linkages
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?
additional information
?
-
cleaves G-MM and G-GM linkages, but nt G-GM linkages
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?
additional information
?
-
-
alginate-lyase is not essential for the production of alginate. When this enzyme is present, as in wild-type cells of Azotobacter vinelandii, its role is restricted to a post-polymerization step, with its activity reaching a maximum in the pres-stationary phase of growth
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alginate
?
-
the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
-
alginate-lyase is not essential for the production of alginate. When this enzyme is present, as in wild-type cells of Azotobacter vinelandii, its role is restricted to a post-polymerization step, with its activity reaching a maximum in the pres-stationary phase of growth
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
Ca2+
-
the activity of isoform AlyA3 is stimulated by Ca2+, an increase by 5fold is observed upon increasing the concentration of Ca2+ from 0.02 mM to 6.3 mM
additional information
-
the activities of isoforms AlyA1 and AlyA2 are not affected by addition of similar concentrations of Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
1 mM ZnCl2 reduces the activity to 7.6% of the control level without Zn2+ added, 0.1 mM Zn2+ reduces the activity to 61%
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the lyase activity is probably stimulated by the epimerase activity forming more guluronate residues at the reducing end of the substrate polymers
-
additional information
the lyase activity is probably stimulated by the epimerase activity forming more guluronate residues at the reducing end of the substrate polymers
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.1 - 8.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7 - 8.4
pH 6.7: about 50% of maximal activity, pH 8.1-8.4: optimum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, also possesses epimerase activity
SwissProt
bifunctional mannuronan C-5-epimerase and alginate lyase, reaction of EC 5.1.3.37
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
strains lacking alyA3 germinate poorly compared to wild type cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
signal peptide is cleaved off, leaving a mature protein of 39000 Da
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D152G
mutation eliminates almost all of both the lyase and epimerase activities
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap SP column chromatography (isoform AlyA1), HiTrap Q column chromatography (isoform AlyA2 and AlyA3), and butyl Sepharose column chromatography (isoform AlyA2)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene algL, construction of a mutant strain SML2, by introductionof a non-polar mutation, with no alginate lyase activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
use of alginate lyase for engineering of alginate polymers for applications in various industrial, agricultural, and medical fields
synthesis
-
alginate production is improved by use of the constructed mutant strain SML2, due to enzyme-deficiency the alginate production reaches a higher level and the alginate polymers have a higher molecular weight
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davidson, I.W.; Lawson, C.J.; Sutherland, I.W.
An alginate lysate from Azotobacter vinelandii phage
J. Gen. Microbiol.
98
223-229
1977
Azotobacter vinelandii, Azotobacter vinelandii phage
Ertesvag, H.; Erlien, F.; Skjak-Braek, G.; Rehm, B.H.A.; Valla, S.
Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase
J. Bacteriol.
180
3779-3784
1998
Azotobacter vinelandii, Azotobacter vinelandii (O52195)
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
Trujillo-Roldan, M.A.; Moreno, S.; Segura, D.; Galindo, E.; Espin, G.
Alginate production by an Azotobacter vinelandii mutant unable to produce alginate lyase
Appl. Microbiol. Biotechnol.
60
733-737
2003
Azotobacter vinelandii
Svanem, B.I.; Strand, W.I.; Ertesvag, H.; Skjak-Braek, G.; Hartmann, M.; Barbeyron, T.; Valla, S.
The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme
J. Biol. Chem.
276
31542-31550
2001
Azotobacter vinelandii, Azotobacter vinelandii (Q9ZFG9)
Trujillo-Roldan, M.A.; Moreno, S.; Espin, G.; Galindo, E.
The roles of oxygen and alginate-lyase in determining the molecular weight of alginate produced by Azotobacter vinelandii
Appl. Microbiol. Biotechnol.
63
742-747
2004
Azotobacter vinelandii
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