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Literature summary extracted from

  • Delpierre, G.; Collard, F.; Fortpied, J.; van Schaftingen, E.
    Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes (2002), Biochem. J., 365, 801-808.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.171 expression in Escherichia coli Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.171 1-deoxy-1-morpholinofructose substrate and competitive inhibitor of fructosamine 3-kinase, doubles the rate of accumulation of glycated haemoglobin, but markedly decreases the amount of haemoglobin containing alkali-labile phosphate Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.171 0.1
-
 1-deoxy-1-morpholin-4-yl-D-fructose 37°C, pH not specified in the publication Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.171 35000
-
 x * 35000, SDS-PAGE Homo sapiens

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 is involved in an intracellular deglycation pathway in human erythrocytes. Spontaneous conversion of fructosamine 3-phosphates into 3-deoxyglucosone ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
 ?
2.7.1.171 ATP + [protein]-N6-D-fructosyl-L-lysine Homo sapiens 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 ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.171 Homo sapiens Q9H479
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.171
-
 Homo sapiens

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.171 ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
-
 Homo sapiens ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
 ?
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 Homo sapiens ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
 ?
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 Homo sapiens ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.171 ? x * 35000, SDS-PAGE Homo sapiens

Synonyms

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