EC Number   |
General Information  |
Reference |
|---|
    5.1.3.37 | evolution |
Ectocarpus contains a multigenic family of putative ManC5-Es. The genome sequence of Ectocarpus offers the opportunity to have access to a higher number of genes, and potentially proteins, 31 putative ManC5-E genes are analyzed. The ManC5-E family includes genes that are differentially regulated during the life cycle of Ectocarpus |
747915 |
| 5.1.3.37 | evolution |
the bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7) |
748180 |
| 5.1.3.37 | malfunction |
reducing the size of AlgE6 influences the epimerization of modified alginates in solution. The A-module from AlgE6 seems to be more affected than AlgE64 at higher degree of oxidation |
747457 |
| 5.1.3.37 | metabolism |
biosynthetic pathway of alginate and the alginate structure involving the enzyme, overview |
746698 |
| 5.1.3.37 | more |
alginate epimerases consist of catalytic and noncatalytic domains. The noncatalytic domains of AlgE4 and AlgE6 possess different alginate binding behavior despite highly similar structures. Noncatalytic subunits of AlgE6 and AlgE4 influence the product specificity of the catalytic domain |
748180 |
| 5.1.3.37 | more |
the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus |
747457 |
| 5.1.3.37 | more |
the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus. AlgE1 is larger than AlgE6 and has two catalytic active modules (A1 and A2) |
747457 |
| 5.1.3.37 | more |
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp. |
747915 |
| 5.1.3.37 | physiological function |
alginate is produced as poly-M and then certain M residues are converted to G by epimerases acting on the polymer level. The alginate-producing bacterium Azotobacter vinelandii has one periplasmic epimerase, which incorporates single G residues into the alginate during secretion of the polymer. In addition, Azotobacter vinelandii produces seven extracellular C-5 alginate epimerases called AlgE1-7. Each of the epimerases convert mannuronic acid to guluronic acid in different patterns. The secreted and calcium-dependent mannuronan C-5 epimerases in Azotobacter vinelandii are responsible for epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in alginate polymers |
748180 |
| 5.1.3.37 | physiological function |
alginate is produced as poly-M and then certain M residues are converted to G by epimerases acting on the polymer level. The alginate-producing bacterium Azotobacter vinelandii has one periplasmic epimerase, which incorporates single G residues into the alginate during secretion of the polymer. In addition, Azotobacter vinelandii produces seven extracellular C-5 alginate epimerases called AlgE1-7. Each of the epimerases converts mannuronic acid to guluronic acid in different patterns. The secreted and calcium-dependent mannuronan C-5 epimerases in Azotobacter vinelandii are responsible for epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in alginate polymers |
748180 |
