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Literature summary extracted from

  • Delpierrre, G.; Vertommen. D.; Communi, D.; Rider, M.H.; van Schaftingen, E.
    Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin (2004), J. Biol. Chem., 279, 27613-27620.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.171 ATP + [protein]-N6-D-fructosyl-L-lysine Homo sapiens fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.171 Homo sapiens
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.171 erythrocyte
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 Homo sapiens
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.171 ATP + [hemoglobin]-N6-D-fructosyl-L-lysine mass-spectrometric identification of the fructosamine residues that are removed from hemoglobin in intact erythrocytes as a result of the action of fructosamine-3-kinase: Lys16, Lys61 and Lys139 in the alpha-chain of hemoglobin, Val1, Lys17, Lys59, Lys66, Lys132, and Lys144 in the beta-chain of hemoglobin. Some (e.g. Lys139 in the alph-chain of hemoglobin) are readily phosphorylated to a maximal extent by fructosamine-3-kinase in vitro whereas others (e.g. Val1 in the beta-chain of hemoglobin) are slowly and only very partially phosphorylated Homo sapiens ADP + [hemoglobin]-N6-(O3-phosphono-D-fructosyl)-L-lysine
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 ?
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 Homo sapiens ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.171 FN3K
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 Homo sapiens
2.7.1.171 fructosamine-3-kinase
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 Homo sapiens