EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
    5.1.3.37 | hepta(beta-(1->4)-D-mannuronate)acid |
poor substrate |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | hexa(beta-(1->4)-D-mannuronate) |
poor substrate |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
alginates from Durvillea antarctica, Lessonia nigrescens, Laminaria hyperborea and a bacterial mannuronan are epimerized. The enzyme converts the M blocks into MGM sequences leaving the G-blocks intact |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
enzyme exhibits a non-random mode of action when acting on mannuronan and alginates of various monomeric compositions. On average 10 residues are epimerised for each enzyme-substrate encounter. A hexameric oligomer is the minimum size to accommodate activity. For hexa-, hepta- and octameric substrates the third M residue from the nonreducing end is epimerised first |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
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 |
? |
- |
? |
| 5.1.3.37 | more |
the enzyme either slides along the alginate chain during catalysis or recognizes a pre-existing G residue as a preferred substrate in its consecutive attacks |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
alginate binding ability of the R-modules of AlgE4 by NMR and isothermal titration calorimetry, overview. Titration of the R-modules with defined alginate oligomers shows strong interaction between AlgE4R and both oligo-M and MG |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
alginate binding ability of the R-modules of AlgE6 by NMR and isothermal titration calorimetry, overview. Titration of the R-modules with defined alginate oligomers shows no interaction between these oligomers and the individual R-modules from AlgE6. Acombination of all three R-modules from AlgE6 shows weak interaction with long M-oligomers |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity |
Azotobacter vinelandii |
? |
- |
? |
| 5.1.3.37 | more |
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. AlgE4 acts processively by sliding along the alginate chain and epimerizing every second residue, generating alternating MG-sequences. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders |
Azotobacter vinelandii |
? |
- |
? |
