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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-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 + N6-D-erythrulosyl-L-lysine
ADP + N6-(O3-phosphono-D-erythrulosyl)-L-lysine
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
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-
-
?
ATP + N6-D-ribulosyl-L-lysine
ADP + N6-(O3-phosphono-D-ribulosyl)-L-lysine
ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
ATP + [lysozyme]-N6-D-psicosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-psicosyl)-L-lysine
in contrast with free psicose-lysine, not all psicosamine residues in the glycated lysozyme substrate would be expected to be accessible to the Fn3KRP active site. In addition, local charge effects may influence the relative affinity for psicosamine residues at different sites in the lysozyme substrate
-
-
?
ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
additional information
?
-
ATP + N6-D-erythrulosyl-L-lysine
ADP + N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-erythrulosyl-L-lysine
ADP + N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-ribulosyl-L-lysine
ADP + N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-ribulosyl-L-lysine
ADP + N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
-
-
-
?
ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
-
-
-
?
ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
-
-
-
?
ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
-
-
-
?
ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-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-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
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-
-
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
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-
-
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-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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?
additional information
?
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-
the enzyme does not act on fructosy-L-lysine or lysozyme glycated with glucose or allose
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?
additional information
?
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-
acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
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?
additional information
?
-
FN3K-RP can act inside erythrocytes as a deglycating enzyme by converting ketoamines into unstable phosphate esters. Potential physiological substrates are psicosamines, which appear to be formed slowly from fructosamines
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?
additional information
?
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-
FN3K-RP can act inside erythrocytes as a deglycating enzyme by converting ketoamines into unstable phosphate esters. Potential physiological substrates are psicosamines, which appear to be formed slowly from fructosamines
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?
additional information
?
-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
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?
additional information
?
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-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
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?
additional information
?
-
FN3K-RP progressively phosphorylates haemoglobin from erythrocytes that had been incubated with allose or ribose
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?
additional information
?
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FN3K-RP progressively phosphorylates haemoglobin from erythrocytes that had been incubated with allose or ribose
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?
additional information
?
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acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
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?
additional information
?
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ribuloseglycine, ribulosevaline and ribuloseleucine are phosphorylated at 510% of the rate observed with 1 mM ribuloselysine, whereas no detectable phosphorylation (<1% of the rate observed with ribuloselysine) is observed with fructoselysine, deoxymorpholinofructose, D-ribulose and D-erythrulose. The purified enzyme does not phosphorylate protein-bound fructosamines, psicosamines or ribulosamine 5-phosphates, but does act on protein-bound ribulosamines and erythrulosamines
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?
additional information
?
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-
acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
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?
additional information
?
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-
acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
-
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?
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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 + [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-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
additional information
?
-
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-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
-
-
?
additional information
?
-
FN3K-RP can act inside erythrocytes as a deglycating enzyme by converting ketoamines into unstable phosphate esters. Potential physiological substrates are psicosamines, which appear to be formed slowly from fructosamines
-
-
?
additional information
?
-
-
FN3K-RP can act inside erythrocytes as a deglycating enzyme by converting ketoamines into unstable phosphate esters. Potential physiological substrates are psicosamines, which appear to be formed slowly from fructosamines
-
-
?
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Collard, F.; Wiame, E.; Bergans, N.; Fortpied, J.; Vertommen, D.; Vanstapel, F.; Delpierre, G.; van Schaftingen, E.
Fructosamine 3-kinase-related protein and deglycation in human erythrocytes
Biochem. J.
382
137-143
2004
Homo sapiens (Q9HA64), Homo sapiens
brenda
Fortpied, J.; Gemayel, R.; Stroobant, V.; van Schaftingen, E.
Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme
Biochem. J.
388
795-802
2005
Arabidopsis thaliana, Spinacia oleracea
brenda
Payne, L.S.; Brown, P.M.; Middleditch, M.; Baker, E.; Cooper, G.J.; Loomes, K.M.
Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5'-[p-(fluorosulfonyl)benzoyl]adenosine
Biochem. J.
416
281-288
2008
Homo sapiens (Q9HA64), 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
Mus musculus (Q8K274), Mus musculus, Homo sapiens (Q9HA64), Homo sapiens
brenda
Gemayel, R.; Fortpied, J.; Rzem, R.; Vertommen, D.; Veiga-da-Cunha, M.; van Schaftingen, E.
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation
FEBS J.
274
4360-4374
2007
Enterococcus faecium, Thermus thermophilus, Lactiplantibacillus plantarum, Staphylococcus aureus
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
Rattus norvegicus
brenda
Inaba, S.I.; Yamaguchi-Goto, M.; Tanaka-Takanaka, K.; Yonesu, K.; Sakurai, H.; Kubota, K.; Izumi, T.
Enzymatic kinetics regarding reversible metabolism of CS-0777, a sphingosine 1-phosphate receptor modulator, via phosphorylation and dephosphorylation in humans
Xenobiotica
48
258-268
2018
Homo sapiens (Q9HA64), Homo sapiens
brenda