EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   2.7.1.52 | ATP + D-arabinose |
28% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | ATP + D-arabinose |
9.3% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | ATP + D-glucose |
2.5% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | ATP + D-glucose |
107% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | ATP + D-ribose |
87% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | ATP + L-arabinose |
31% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | ATP + L-rhamnose |
41% of the activity with L-fucose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | more |
less than 5% of the activity with L-fucose is observed with: D-mannose, D-galactose, D-xylose, L-xylose, D-fucose and L-fucolose |
Sus scrofa |
? |
- |
? |
| 2.7.1.52 | more |
enzyme generates GDP-L-fucose from L-fucose 1-phosphate and GTP. No substrates for fucokinase activity are: L-arabinose, glucose, galactose, mannose, xylose, L-rhamnose, galactosamine, glucosamine, N-acetylglucosamine |
Arabidopsis thaliana |
? |
- |
? |
| 2.7.1.52 | more |
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview |
Bacteroides fragilis |
? |
- |
? |
