Application | Comment | Organism |
---|---|---|
medicine | 1,2-alpha-L-fucosynthase, derived from an inverting alpha-glycosidase (AfcA) and from a glycosidase with an unusual reaction mechanism, may serve as a promising tool to create biologically active compounds that can be used not only for prebiotics but also for clinical treatments aimed to regulate various cellular processes and infectious diseases | Bifidobacterium bifidum |
Cloned (Comment) | Organism |
---|---|
wild-type and mutant derivatives of the catalytic domain of AfcA (Fuc domain) | Bifidobacterium bifidum |
Protein Variants | Comment | Organism |
---|---|---|
D766G | most effectively synthesizes 2'-fucosyllactose | Bifidobacterium bifidum |
N421G | synthesizes 2'-fucosyllactose | Bifidobacterium bifidum |
N423G | synthesizes 2'-fucosyllactose | Bifidobacterium bifidum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bifidobacterium bifidum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant derivatives of the catalytic domain of AfcA (Fuc domain) | Bifidobacterium bifidum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2'-fucosyllactose + H2O | hydrolysis by the Fuc domain of AfcA. N423 and D766 are critical for activating an attacking water molecule and N421 is critical for maintaining the water molecule and the side-chain of E566 (a general acid) in their proper orientations | Bifidobacterium bifidum | ? | - |
? | |
beta-L-fucosyl fluoride + lactose + H2O | Hehre resynthesis-hydrolysis is catalyzed by the wild-type Fuc domain of AfcA. Conversion of the inverting alpha-glycosidase to a glycosynthase | Bifidobacterium bifidum | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AfcA | - |
Bifidobacterium bifidum |