Application | Comment | Organism |
---|---|---|
synthesis | to overcome the poor solubility of FutA upon expression in Escherichia coli, codon optimization, and systematic truncation of the protein at the C-terminus with only one heptad repeat remaining yield 150-200 mg/l of soluble protein of FutA and result in more than an 18fold increase in the 3-fucosyllactose yield. Mutant A128N obtained by focused directed evolution mutant displays a 3.4fold higher catalytic activity than wild-type FutA. Mutant A128N/H129E/Y132I exhibits a 9.6fold improvement in specific activity when compared to wild-type. Mutants A128N/H129E/S46F and A128N/H129E/Y132I/S46F show synergistic effects, that is 14.5- and 15.5fold improvement in specific activity relative to wild-type. The mutations increase the binding affinity for lactose and kcat values for lactose and GDP-fucose. The quadruple mutant A128N/H129E/Y132I/S46F synthesizes 3-fucosyllactose with an improved yield and productivity (more than 96% yield based on 5 mM of GDP-Fuc within 1 h) | Helicobacter pylori |
Cloned (Comment) | Organism |
---|---|
expresssion in Escherichia coli | Helicobacter pylori |
Protein Variants | Comment | Organism |
---|---|---|
A128N | mutant obtained by focused directed evolution mutant, 3.4fold higher catalytic activity than wild-type | Helicobacter pylori |
A128N/H129E/S46F | 14.5fold improvement in specific activity | Helicobacter pylori |
A128N/H129E/Y132I | 9.6fold improvement in specific activity | Helicobacter pylori |
A128N/H129E/Y132I/S46F | 15.5fold improvement in specific activity | Helicobacter pylori |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Helicobacter pylori | O25142 | - |
- |
Helicobacter pylori 26695 | O25142 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
FutA | - |
Helicobacter pylori |
HP_0379 | - |
Helicobacter pylori |