Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Azotobacter vinelandii |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
57700 | - |
x * 57700, calculated | Azotobacter vinelandii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azotobacter vinelandii | Q44493 | - |
- |
Subunits | Comment | Organism |
---|---|---|
? | x * 57700, calculated | Azotobacter vinelandii |
Synonyms | Comment | Organism |
---|---|---|
AlgE4 | - |
Azotobacter vinelandii |
poly(beta-D-mannuronate) C5 epimerase 4 | - |
Azotobacter vinelandii |