EC Number   |
Natural Substrates |
|---|
   2.7.1.171 | ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one |
CS-0777 |
| 2.7.1.171 | ATP + [protein]-N5-D-ribulosyl-L-lysine |
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
- |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Spontaneous conversion of fructosamine 3-phosphates into 3-deoxyglucosone |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone. This pathway appears to dominate 3-deoxyglucosone production in vivo, making it possible to modulate 3-deoxyglucosone levels by stimulating or inhibiting the reaction |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as protein-bound fructoselysines. The fructosamine most frequently encountered in nature is fructoselysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins and protecting cells from the deleterious effects of nonenzymatic glycation |
| 2.7.1.171 | ATP + [protein]-N6-D-fructosyl-L-lysine |
protein repair mechanism. Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates. The latter are unstable and spontaneously decompose into inorganic phosphate and 3-deoxyglucosone, with concomitant regeneration of the unglycated amine |
