Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Agrobacterium tumefaciens |
Crystallization (Comment) | Organism |
---|---|
crystal structures of native protein and its inactive mutant H531A in complex with alginate trisaccharide, at 2.10 and 2.99 A resolutions with final R-factors of 18.3 and 19.9%, respectively. The enzyme is comprised of an alpha/alpha-barrel plus anti-parallel beta-sheet as a basic scaffold. His311 and Tyr365 are the catalytic base and acid, respectively. A short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains are essential for the exolytic mode of action | Agrobacterium tumefaciens |
Protein Variants | Comment | Organism |
---|---|---|
H311A | 0.3% of wild-type activity | Agrobacterium tumefaciens |
H531A | inactive | Agrobacterium tumefaciens |
R199A | 4.3% of wild-type activity | Agrobacterium tumefaciens |
W467A | 0.45% of wild-type activity | Agrobacterium tumefaciens |
Y365F | 0.011% of wild-type activity | Agrobacterium tumefaciens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Agrobacterium tumefaciens | A9CEJ9 | polysaccharide lyase family 15 | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.14 | - |
wild-type, pH 7.5, 30°C | Agrobacterium tumefaciens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-L-guluronosyl linkage in alginate | - |
Agrobacterium tumefaciens | ? | - |
? |