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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
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
malfunction

-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
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
-
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
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, protein–protein 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
-
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
-
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
-
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
-
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
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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
-
-
?
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 + 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-(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
?
-
-
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
?
-
-
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 + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
Q9HA64
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
Q9HA64
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
Q9H479
-
-
-
?
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
Q9H479
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
Q9H479
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.
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Pascal, S.M.; Veiga-da-Cunha, M.; Gilon, P.; van Schaftingen, E.; Jonas, J.C.
Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations
Am. J. Physiol. Endocrinol. Metab.
298
E586-596
2009
Mus musculus, Mus musculus (Q9ER35)
brenda
van Schaftingen, E.; Collard, F.; Wiame, E.; Veiga-da-Cunha, M.
Enzymatic repair of Amadori products
Amino Acids
42
1143-1150
2012
Homo sapiens, Mus musculus
brenda
Krause, R.; Oehme, A.; Wolf, K.; Henle, T.
A convenient HPLC assay for the determination of fructosamine-3-kinase activity in erythrocytes
Anal. Bioanal. Chem.
386
2019-2025
2006
Homo sapiens
brenda
Conner, J.R.; Beisswenger, P.J.; Szwergold, B.S.
The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinase-related protein appears to be constitutive and unaffected by environmental signals
Biochem. Biophys. Res. Commun.
323
932-936
2004
Homo sapiens
brenda
Delpierre, G.; Collard, F.; Fortpied, J.; van Schaftingen, E.
Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes
Biochem. J.
365
801-808
2002
Homo sapiens, Homo sapiens (Q9H479)
brenda
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
Biochem. J.
399
257-264
2006
Mus musculus (Q9ER35)
brenda
Brown, T.R.; Su, B.; Brown, K.A.; Schwartz, M.A.; Tobia, A.M.; Kappler, F.
Modulation of in vivo 3-deoxyglucosone levels
Biochem. Soc. Trans.
31
1433-1437
2003
Rattus norvegicus
brenda
Delpierre, G.; Veiga-da-Cunha, M.; Vertommen, D.; Buysschaert, M.;, Van Schaftingen E.
Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites
Diabetes Metab.
32
31-39
2005
Homo sapiens, Homo sapiens (Q9H479)
brenda
Delpierre, G.; Rider, M.H.; Collard, F.; Stroobant, V.; Vanstapel, F.; Santos, H.; van Schaftingen, E.
Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase
Diabetes
49
1627-1634
2000
Homo sapiens, Homo sapiens (Q9H479), Mus musculus, Mus musculus (Q9ER35)
brenda
Szwergold, B.S.; Howell, S.; Beisswenger, P.J.
Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo
Diabetes
50
2139-2147
2001
Homo sapiens
brenda
Collard, F.; Delpierre, G.; Stroobant, V.; Matthijs, G.; van Schaftingen, E.
A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines
Diabetes
52
2888-2895
2004
Homo sapiens, Homo sapiens (Q9HA64), Mus musculus, Mus musculus (Q8K274)
brenda
Mohas, M.; Kisfali, P.; Baricza, E.; Merei, A.; Maasz, A.; Cseh, J.; Mikolas, E.; Szijarto, I.A.; Melegh, B.; Wittmann, I.
A polymorphism within the fructosamine-3-kinase gene is associated with HbA1c levels and the onset of type 2 diabetes mellitus
Exp. Clin. Endocrinol. Diabetes
118
209-212
2009
Homo sapiens, Homo sapiens (Q9H479)
brenda
Notarnicola, M.; Caruso, M.G.; Tutino, V.; Guerra, V.; Frisullo, S.; Altomare, D.F.; Misciagna, G.
Reduced fructosamine-3-kinase activity and its mRNA in human distal colorectal carcinoma
Genes Nutr.
5
257-262
2010
Homo sapiens
brenda
Delpierrre, G.; Vertommen. D.; Communi, D.; Rider, M.H.; van Schaftingen, E.
Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin
J. Biol. Chem.
279
27613-27620
2004
Homo sapiens
brenda
Delplanque, J.; Delpierre, G.; Opperdoes, F.R.; van Schaftingen, E.
Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein
J. Biol. Chem.
279
46606-46613
2004
Gallus gallus, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Caruso, M.G.; Notarnicola, M.; Altomare, D.F.; Misciagna, G.
Gene expression of fructosamine 3 kinase in patients with colorectal cancer
Oncology
73
72-75
2008
Homo sapiens
brenda
Hellwig, A.; Scherber, A.; Koehler, C.; Hanefeld, M.; Henle, T.
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes
Clin. Chem. Lab. Med.
52
93-101
2014
Homo sapiens (Q9H479)
-
brenda
Avemaria, F.; Carrera, P.; Lapolla, A.; Sartore, G.; Chilelli, N.C.; Paleari, R.; Ambrosi, A.; Ferrari, M.; Mosca, A.
Possible role of fructosamine 3-kinase genotyping for the management of diabetic patients
Clin. Chem. Lab. Med.
53
1315-1320
2015
Homo sapiens, Homo sapiens (Q9H479)
brenda
Cikomola, J.C.; Kishabongo, A.S.; Vandepoele, K.; Mulder, M.; Katchunga, P.B.; Laukens, B.; Schie, L.V.; Grootaert, H.; Callewaert, N.; Speeckaert, M.M.; Delanghe, J.R.
A simple colorimetric assay for measuring fructosamine 3 kinase activity
Clin. Chem. Lab. Med.
55
154-159
2017
Homo sapiens, Homo sapiens (Q9H479)
brenda
Skrha, J.; Muravska, A.; Flekac, M.; Horova, E.; Novak, J.; Novotny, A.; Prazny, M.; Skrha, J.; Kvasnicka, J.; Landova, L.; Jachymova, M.; Zima, T.; Kalousova, M.
Fructosamine 3-kinase and glyoxalase I polymorphisms and their association with soluble RAGE and adhesion molecules in diabetes
Physiol. Res.
63 Suppl 2
S283-S291
2014
Homo sapiens, Homo sapiens (Q9H479)
brenda