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Literature summary for 2.7.1.171 extracted from

  • Veiga da-Cunha, M.; Jacquemin, P.; Delpierre, G.; Godfraind, C.; Theate, I.; Vertommen, D.; Clotman, F.; Lemaigre, F.; Devuyst, O.; van Schaftingen, E.
    Increased protein glycation in fructosamine 3-kinase-deficient mice (2006), Biochem. J., 399, 257-264.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

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
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Organism

Organism UniProt Comment Textmining
Mus musculus Q9ER35
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Substrates and Products (Substrate)

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
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Synonyms

Synonyms Comment Organism
FN3K
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Mus musculus

General Information

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, protein–protein interaction or recognition sites for phosphorylation (which often comprise basic residues) or ubiquitinylation Mus musculus