Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [protein]-N6-D-fructosyl-L-lysine | Mus musculus | FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine | ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q9ER35 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Mus musculus | ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FN3K | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | Fn3k-/- mice look healthy and have normal blood glucose and serum fructosamine levels. Their level of haemoglobin-bound fructosamines is approx. 2.5-fold higher than that of control (Fn3k+/+) or Fn3k+/- mice. Other intracellular proteins are also significantly more glycated in Fn3k-/- mice in erythrocytes and in brain, kidney, liver and skeletal muscle, indicating that FN3K removes fructosamines from intracellular proteins in vivo | Mus musculus |
physiological function | FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine. Repairing lysine residues may be important to restore enzymatic activity, proteinprotein interaction or recognition sites for phosphorylation (which often comprise basic residues) or ubiquitinylation | Mus musculus |