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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.2.3 | gene algE1-1 | Azotobacter vinelandii |
5.1.3.37 | - |
Azotobacter vinelandii |
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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.2.3 | additional information | - |
additional information | kinetics | Azotobacter vinelandii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
4.2.2.3 | extracellular | secretion | Azotobacter vinelandii | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.2.2.3 | Ca2+ | dependent on | Azotobacter vinelandii |
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 | - |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.2.2.3 | culture medium | - |
Azotobacter vinelandii | - |
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 | ? | - |
? |
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 |