Any feedback?
Literature summary for 5.1.3.37 extracted from
- Single-molecular pair unbinding studies of mannuronan C-5 epimerase AlgE4 and its polymer substrate (2004), Biomacromolecules, 5, 1288-1295.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Azotobacter vinelandii |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 57700 | - |
x * 57700, calculated | Azotobacter vinelandii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Azotobacter vinelandii | Q44493 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 57700, calculated | Azotobacter vinelandii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AlgE4 | - |
Azotobacter vinelandii |
| poly(beta-D-mannuronate) C5 epimerase 4 | - |
Azotobacter vinelandii |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
