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Literature summary extracted from

  • 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 (2001), J. Biol. Chem., 276, 31542-31550.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.2.3 additional information the lyase activity is probably stimulated by the epimerase activity forming more guluronate residues at the reducing end of the substrate polymers Azotobacter vinelandii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.3 gene algE1-1 Azotobacter vinelandii
5.1.3.37
-
 Azotobacter vinelandii

Protein Variants

EC Number Protein Variants Comment Organism
4.2.2.3 D152G nearly inactive mutant Azotobacter vinelandii
4.2.2.3 D152G mutation eliminates almost all of both the lyase and epimerase activities Azotobacter vinelandii
5.1.3.37 D152G mutation eliminates almost all of both the lyase and epimerase activities Azotobacter vinelandii
5.1.3.37 additional information a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7 Azotobacter vinelandii
5.1.3.37 additional information a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7 Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.3 additional information
-
 additional information kinetics Azotobacter vinelandii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.2.3 extracellular secretion Azotobacter vinelandii
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.2.3 Ca2+ dependent on Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Azotobacter vinelandii
-
 bifunctional enzyme comprising alginate lyase activity as well as mannuronan C-5-epimerase activity
-
4.2.2.3 Azotobacter vinelandii Q9ZFG9 bifunctional mannuronan C-5-epimerase and alginate lyase, reaction of EC 5.1.3.37
-
5.1.3.37 Azotobacter vinelandii Q44494
-
-
5.1.3.37 Azotobacter vinelandii Q9ZFG9 bifunctional mannuronan C-5-epimerase and alginate lyase, reaction of EC 4.2.2.3
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.2.3 R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1 alginate lyase activity and mannuronan C-5-epimerase activity of the bifunctional enzyme might use the same active site Azotobacter vinelandii
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.2.3 culture medium
-
 Azotobacter vinelandii
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.3 alginate 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 Azotobacter vinelandii oligouronides
-
 ?
4.2.2.3 alginate substrate from brown algae Macrocystis pyrifera rich in polymannuronate and polyguluronate, cleavage sequences are G-/-MM and/or G-/-GM Azotobacter vinelandii oligosaccharides of 4-7 monomers
-
 ?
4.2.2.3 additional information substrate specificity Azotobacter vinelandii ?
-
 ?
5.1.3.37 additional information 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 Azotobacter vinelandii ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 AlgE7
-
 Azotobacter vinelandii
4.2.2.3 alginate lyase
-
 Azotobacter vinelandii
4.2.2.3 More enzyme belongs to the family of secreted Ca2+-dependent epimerases Azotobacter vinelandii
5.1.3.37 AlgE1
-
 Azotobacter vinelandii
5.1.3.37 AlgE7
-
 Azotobacter vinelandii