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ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
CS-0777
-
-
ir
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
ATP + 1-deoxy-1-morpholin-4-yl-D-psicose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-psicose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-ribulose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-ribulose
-
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
ATP + N-alpha-hippuryl-N-epsilon-psicosyllysine
ADP + ?
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
ATP + N2-(1-deoxy-D-fructosyl)-glycylglycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycylglycine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-L-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-L-valine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
ATP + N5-D-fructosyl-L-ornithine
ADP + N5-(O3-phosphono-D-fructosyl)-L-ornithine
-
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-L-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-L-lysine
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
ATP + N6-D-fructosyl-L-lysine
ADP + N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
-
-
-
?
ATP + Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine
ADP + Nalpha-hippuryl-Nepsilon-(1-deoxy-3-phospho-D-fructosyl)lysine
-
-
Nalpha-hippuryl-Nepsilon-(3-phosphofructosyl)lysine like other 3-phosphofructosylamines, is not stable. Terminating the enzyme reaction with trichloracetic acid stabilises the analyte
-
?
ATP + [hemoglobin]-N6-D-fructosyl-L-lysine
ADP + [hemoglobin]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
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
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?
glycated bovine serum albumin + ATP
?
derived from dialyzed glycated bovine serum albumin
-
-
?
additional information
?
-
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
-
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
-
Vmax is 35% of the value for N6-D-fructosyl-L-lysine
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
repairing glucose-mediated non-enzymatic modification of proteins. The function of fructosamine-3-kinase is seen in catalysing the ATP-dependent phosphorylation of the protein-bound fructosamine (Amadori compound) fructoselysine, which is the first stable intermediate resulting from the Maillard reaction between glucose and lysine, on its 3-hydroxy group to 3-phosphofructosyllysine. The phosphorylation destabilises the fructose-amine linkage leading to a spontaneous decomposition of 3-phosphofructosyllysine to the unmodified lysine residue as well as to 3-deoxyglucosulose and inorganic phosphate
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
[histone]-N6-D-fructosyl-L-lysine, [hemoglobin]-N6-D-fructosyl-L-lysine. Similar experiments with other glycated proteins, including bovine serum albumin, and lysozyme indicate that fructoselysine residues on glycated proteins are readily phosphorylated by fructosamine 3-kinase, apparently irrespective of the protein. Phosphorylation destablilizes the fructoselysine adduct and leads to its spontaneous decomposition
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
additional information
?
-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
-
-
?
additional information
?
-
-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
-
-
?
additional information
?
-
-
the kinase is specific for 1-deoxy-1-amino fructose adducts and does not catalyze phosphorylation of other monosaccharides and polyols, such as glucose, galactose, mannose, glucosamine, galactosamine, or myo-inositol
-
-
?
additional information
?
-
development of a PLC-based assay with substrate N-alpha-hippuryl-N-epsilon-psicosyllysine for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes, method evaluation, overview
-
-
?
additional information
?
-
development of a simple colorimetric method for assaying FN3K activity in human body fluids
-
-
?
additional information
?
-
-
development of a simple colorimetric method for assaying FN3K activity in human body fluids
-
-
?
additional information
?
-
the fructosamines bound to Lys139alpha, located near the C-terminus of the alpha subunits, and Lys16alpha, located on a loop of the alpha subunits, are good substrates. The N-terminal glycated valine is a poor substrate, consistent with free fructosevaline being a much poorer substrate than free fructoselysine
-
-
?
additional information
?
-
-
the fructosamines bound to Lys139alpha, located near the C-terminus of the alpha subunits, and Lys16alpha, located on a loop of the alpha subunits, are good substrates. The N-terminal glycated valine is a poor substrate, consistent with free fructosevaline being a much poorer substrate than free fructoselysine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
CS-0777
-
-
ir
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
repairing glucose-mediated non-enzymatic modification of proteins. The function of fructosamine-3-kinase is seen in catalysing the ATP-dependent phosphorylation of the protein-bound fructosamine (Amadori compound) fructoselysine, which is the first stable intermediate resulting from the Maillard reaction between glucose and lysine, on its 3-hydroxy group to 3-phosphofructosyllysine. The phosphorylation destabilises the fructose-amine linkage leading to a spontaneous decomposition of 3-phosphofructosyllysine to the unmodified lysine residue as well as to 3-deoxyglucosulose and inorganic phosphate
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
the FN3K gene may have arisen by an event of duplication of an ancestral gene, FN3K-related protein (FN3K-RP). The gene encoding FN3K-RP is located next to the one encoding FN3K, and share a 65% sequence homology with FN3K and an identical genome organization. Both FN3K and FN3K-RP phosphorylate psicosamines and ribulosamines, but only the former act on fructosamines
evolution
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fructosamine-3-kinases belong to the large superfamily of protein kinase-like (PKL) enzymes. The strained disulfides in the dimeric Arabidosis thalina enzyme function as redox switches to reversibly regulate the activity and dimerization of FN3K. Human FN3K, which contains an equivalent P-loop Cys, is also redox sensitive, whereas ancestral bacterial FN3K homologues, which lack a P-loop Cys, are not. Redox control mediated by the P-loop Cys is an ancient mechanism of FN3K regulation that emerged progressively during FN3K evolution from bacteria to humans. Redox regulation seem to have evolved in FN3K homologues in response to changing cellular redox conditions
evolution
fructosamine-3-kinases belong to the large superfamily of protein kinase-like (PKL) enzymes. The strained disulfides in the dimeric Arabidosis thalina enzyme function as redox switches to reversibly regulate the activity and dimerization of FN3K. Human FN3K, which contains an equivalent P-loop Cys, is also redox sensitive, whereas ancestral bacterial FN3K homologues, which lack a P-loop Cys, are not. Redox control mediated by the P-loop Cys is an ancient mechanism of FN3K regulation that emerged progressively during FN3K evolution from bacteria to humans. Redox regulation seems to have evolved in FN3K homologues in response to changing cellular redox conditions
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
malfunction
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mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
malfunction
significant relationship of FN3K (rs1056534) and (rs3848403) polymorphisms with with endothelial dysfunction and concentration of soluble receptor for advanced glycation end-products (sRAGE) in patients with diabetes, clinical parameters, overview
malfunction
FN3K CRISPR knockout alters redox-sensitive cellular metabolites
malfunction
N-acetyl cysteine treatment partially rescues the effects of FN3K loss on NRF2 driven tumor phenotypes. FN3K deficiency increases NRF2 glycation and impairs its ability to counter ROS stress in liver and lung cancer cells. Pre-treatment with the ROS scavenger and GSH precursor N-acetyl cysteine (NAC) reverses H2O2 and DLS toxicity and restores glutathione balance in FN3K-deficient HepG2 and H3255 cells, respectively. FN3K deficiency leads to increased proteasomal and MG132-sensitive degradation of the glycated NRF2 protein. Glycation also affects NRF2 function in KEAP1 mutant cells, for example gene and protein expression analyses of FN3K deficient and control Huh-1 liver cancer cells (KEAP1N414Y) show loss of NRF2 targets and resultant redox imbalance as indicated by increased glutathione oxidation
malfunction
polymorphisms of the FN3K gene are associated with variations in HbA1c levels and with the onset of type 2 diabetes mellitus (T2DM) and pathogenic mechanisms related to its complications, role of FN3K polymorphisms in the development of microvascular and macrovascular complications of diabetes, overview. The FN3K genotype presenting GG at position -385, TT at position -232, and CC at c.900 A, is associated with less severe microangiopathic and macroangiopathic complications as a whole, compared to all other genotypes
malfunction
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removal of the chloroplast signal peptide results in the localization of AtFN3K in different cellular compartments, including nucleus and mitochondria. FN3K CRISPR knockout alters redox-sensitive cellular metabolites
metabolism
despite its ability to reduce the glycation of intracellular islet proteins, fructosamine-3-kinase is neither required for the maintenance of beta-cell survival and function under control conditions nor involved in protection against beta-cell glucotoxicity
metabolism
starvation and diabetes do not change the level of expression of FN3K in different tissues, and no regulation of FN3K expression is observed in human fibroblasts treated with condition mimicking the diabetic state
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
physiological function
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
physiological function
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
physiological function
advanced glycation end-products are key players in pathogenesis of long-term vascular diabetes complications, several enzymes such as fructosamine 3-kinase (FN3K) and glyoxalase I (GLO I) are crucial in preventing glycation processes
physiological function
fructosamine 3 kinase is a deglycating enzyme, which may play a key role in reducing diabetes-induced organ damage by removing bound glucose from glycated proteins
physiological function
fructosamine 3-kinase (FN3K) is involved in protein deglycation FN3K phosphorylates fructosamines on the third carbon of their sugar moiety, making them unstable and causing them to detach from proteins, suggesting a protective role of this enzyme. FN3K is able to break down the second intermediate of the non-enzymatic glycation cascade by phosphorylating fructoselysine to a fructoselysine-3-phosphate. The variability in FN3K activity is associated with some polymorphisms in the FN3K gene, FN3K involvement in diabetes, overview. FN3K might act in concert with other molecular mechanisms and may impact on gene expression and activity of other enzymes involved in deglycation process
physiological function
impact on glycation, and possibly on diabetic complications, is attributed to fructosamine-3-kinase (FN3K) and its related protein (FN3K-RP) because they degrade Amadori compounds in vivo. Individual differences in FN3K-RP activity might contribute to an individual risk for diabetic complications
physiological function
CS-0777, a candidate compound for autoimmune diseases, becomes phosphorylated to an active metabolite, M1, by fructosamine 3-kinase (FN3K) and FN3K-related protein (FN3K-RP, EC 2.7.1.172), and (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate is reverted back to CS-0777 by alkaline phosphatase (ALP) in the body
physiological function
fructosamine-3-kinase (FN3K) is a kinase that triggers protein deglycation. Transcription factor NRF2 activity depends on FN3K activity, NRF2 transcription factor controls a cell stress program that is implicated in cancer. Role for the glycation of cellular proteins and implicates FN3K as targetable modulator of NRF2 activity in cancer. The development of hepatocellular carcinoma triggered by MYC and Keap1 inactivation depends on FN3K in vivo, role of FN3K-sensitive NRF2 glycation in liver cancer in vivo, overview
physiological function
fructosamine-3-kinase (FN3K) is involved in deglycation, active in removing ketoamines, and preventing advanced glycation end product production. Enzyme FN3K is capable of counteracting the effect of hyperglycemia by intervening in protein glycation. The FN3K genetic variability is linked to the enzyme's enzymatic activity and glycated hemoglobin (HbA1c) levels
physiological function
fructosamine-3-kinase (FN3K) is involved in natural cellular repair mechanisms to control non-enzymatic glycation of proteins. It also has potential in the disruption of retinal advanced glycation end products (AGEs), which are important risk factor in pathogenesis in complement, lipid, angiogenic, inflammatory and extracellular matrix pathways in the eye. Increased levels of AGEs have been found in the Bruch's membrane, retinal pigment epithelium (RPE) and drusen of patients with age-related macular degeneration (AMD), a degenerative disorder of the macular region of the retina. Analysis of FN3K treatment of AGE-modified neural porcine, murine, and human retinas. The treatment reduces AGE-related autofluorescence. Murine and human eyes treated intravitreally with FN3K show less drusenoid material and lesions on stained tissue sections. Biochemical changes after FN3K treatment, overview. Near-infrared (NIR) microspectroscopy of the Bruch's membrane and drusen on hematoxylin and eosin stained slides originating from two patients with stage 3 age-related macular degeneration (AMD). Vivo intravitreal FN3K treatment on human eyes strongly reduces size of subretinal drusenoid deposits on optical coherence tomography
physiological function
variations in the level of the deglycating enzyme fructosamine-3-kinase (FN3K) might be associated with the glycation gap (GGap), a phenomenon of a discrepancy between glycated hemoglobin levels and other indicators of average glycemia may be due to many factors. GGap is associated with differences in complications in patients with diabetes and may possibly be explained by dissimilarities in deglycation in turn leading to altered production of advanced glycation end products (AGEs). Increased erythrocyte FN3K concentrations and enzyme activity (323%) are determined in a population dichotomized for a large positive or negative GGap. This is associated with lower AGE levels in the negative-GGap group (79%), lower proinflammatory adipokines (leptin-to-adiponectin ratio) (73%), and much lower prothrombotic PAI-1 levels (19%). FN3K may play a key role in the GGap and thus diabetes complications
additional information
no correlations of enzyme activity with age, sex, body weight, blood cholesterol, or plasma glucose in an oral glucose tolerance test are observed. Subjects whose parents or siblings had a stroke show lower FN3K activity
additional information
the strained disulfides in the dimeric Arabidosis thalina enzyme function as redox switches to reversibly regulate the activity and dimerization of FN3K. Critical role for the ATP-binding P-loop in the redox regulation of FN3Ks. HsFN3K, in which the P-loop Cys is conserved, is redox-regulated and displayed altered oligomerization when proliferating cells are exposed to acute oxidative stress. Structure-function analysis, overview
additional information
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the strained disulfides in the dimeric Arabidosis thalina enzyme function as redox switches to reversibly regulate the activity and dimerization of FN3K. Critical role for the ATP-binding P-loop in the redox regulation of FN3Ks. The P-loop is stabilized in an extended conformation by a Cys-mediated disulfide bond connecting two chains to form a covalently linked dimer in which the reduction of disulfides results in AtFN3K activation. Structure-function analysis, overview
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C236A
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site-directed mutagenesis, similar to the wild-type enzyme, both dimeric and monomeric forms are detected
C236S
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site-directed mutagenesis, similar to the wild-type enzyme, both dimeric and monomeric forms are detected
C32A
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site-directed mutagenesis, similar to the wild-type enzyme, both dimeric and monomeric forms are detected
C32A/C236A/C196A
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site-directed mutagenesis, similar to the wild-type enzyme, both dimeric and monomeric forms are detected
C32S
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site-directed mutagenesis, similar to the wild-type enzyme, both dimeric and monomeric forms are detected
additional information
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diabetic subjects with the CC variant of SNP rs1056534 (G900C), which is associated with a higher FN3K activity, have lower HbA1c levels compared with other genotypes
additional information
the G900C (rs1056534) single nucleotide polymorphism of the FN3K gene is associated with the enzyme activity, with the level of HbA and the onset of the disease, but not with either of the diabetic microvascular complications
additional information
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the G900C (rs1056534) single nucleotide polymorphism of the FN3K gene is associated with the enzyme activity, with the level of HbA and the onset of the disease, but not with either of the diabetic microvascular complications
additional information
analysis of the FN3K gene on a Caucasian cohort of diabetic patients, molecular characterization of the FN3K gene by analyzing its promoter and of polymorphisms, c-385A/G (rs3859206) and the c-232A/T (rs2256339), associated with FN3K enzymatic activity in erythrocytes, as well as two variants c-421C/T and c-429delATCGGAG
additional information
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analysis of the FN3K gene on a Caucasian cohort of diabetic patients, molecular characterization of the FN3K gene by analyzing its promoter and of polymorphisms, c-385A/G (rs3859206) and the c-232A/T (rs2256339), associated with FN3K enzymatic activity in erythrocytes, as well as two variants c-421C/T and c-429delATCGGAG
additional information
while GG and CG genotypes of rs1056534 with mutated G allele are associated with significant decrease of sRAGE, in rs3848403 polymorphism TT genotype with mutated T allele is related with significant sRAGE increase
additional information
-
while GG and CG genotypes of rs1056534 with mutated G allele are associated with significant decrease of sRAGE, in rs3848403 polymorphism TT genotype with mutated T allele is related with significant sRAGE increase
additional information
allelic variants of FN3K polymorphisms revealed 13 distinct genotypic variants in a cohort of patients with type 2 diabetes mellitus (T2DM), detection of three polymorphisms associated with the enzymatic activity (rs3859206 and rs2256339 in the promoter region and rs1056534 in exon 6). The FN3K genotype presenting GG at position -385, TT at position -232, and CC at c.900 A, is associated with less severe microangiopathic and macroangiopathic complications as a whole, compared to all other genotypes
additional information
-
allelic variants of FN3K polymorphisms revealed 13 distinct genotypic variants in a cohort of patients with type 2 diabetes mellitus (T2DM), detection of three polymorphisms associated with the enzymatic activity (rs3859206 and rs2256339 in the promoter region and rs1056534 in exon 6). The FN3K genotype presenting GG at position -385, TT at position -232, and CC at c.900 A, is associated with less severe microangiopathic and macroangiopathic complications as a whole, compared to all other genotypes
additional information
knockdown of FN3K with two different shRNAs in HepG2 cells and in H3255 cells. The mutant cells have higher levels of NRF2, and both FACS assay and immunoblot show reduction of NRF2 protein upon knockdown of either FN3K or NRF2. FN3K deficiency leads to increased proteasomal and MG132-sensitive degradation of the glycated NRF2 protein
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Enzymatic repair of Amadori products
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Modulation of in vivo 3-deoxyglucosone levels
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Rattus norvegicus
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Homo sapiens (Q9H479), Homo sapiens
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Mus musculus (Q9ER35), Mus musculus, Homo sapiens (Q9H479), Homo sapiens
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Homo sapiens
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Diabetes
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Mus musculus (Q8K274), Mus musculus, Homo sapiens (Q9HA64), Homo sapiens
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Mohas, M.; Kisfali, P.; Baricza, E.; Merei, A.; Maasz, A.; Cseh, J.; Mikolas, E.; Szijarto, I.A.; Melegh, B.; Wittmann, I.
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Homo sapiens (Q9H479), Homo sapiens
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Gene expression of fructosamine 3 kinase in patients with colorectal cancer
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Homo sapiens
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Arabidopsis thaliana, Homo sapiens (Q9H479)
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