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Literature summary extracted from
- Single-molecular pair unbinding studies of mannuronan C-5 epimerase AlgE4 and its polymer substrate (2004), Biomacromolecules, 5, 1288-1295.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.3.37 | expression in Escherichia coli | Azotobacter vinelandii |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.1.3.37 | Dynamic Force Spectroscopy. The position of the activation barrier is 0.23 nm for the AlgE4 and 0.10 nm for its A-module. The lack of interaction observed between the R-module and mannuronan suggest that the A-module contains the binding site for the polymer substrate. The ratio between the epimerase-mannuronan dissociation rate and the catalytic rate for epimerization of single hexose residues suggests a processive mode of action of the AlgE4 epimerase yielding the observed sequence pattern in the uronan associated with the A-module of this enzyme | Azotobacter vinelandii |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.3.37 | 57700 | - |
x * 57700, calculated | Azotobacter vinelandii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.3.37 | Azotobacter vinelandii | Q44493 | - |
- |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.3.37 | ? | x * 57700, calculated | Azotobacter vinelandii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.3.37 | AlgE4 | - |
Azotobacter vinelandii |
| 5.1.3.37 | poly(beta-D-mannuronate) C5 epimerase 4 | - |
Azotobacter vinelandii |
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Release 2023.1 (January 2023)
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